Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity
Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Meng, Xiangfeng [verfasserIn] |
|---|
| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2018 |
|---|
| Schlagwörter: |
|---|
| Anmerkung: |
© Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
|---|
| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer Berlin Heidelberg, 1984, 102(2018), 18 vom: 24. Juli, Seite 7935-7950 |
|---|---|
| Übergeordnetes Werk: |
volume:102 ; year:2018 ; number:18 ; day:24 ; month:07 ; pages:7935-7950 |
| Links: |
|---|
| DOI / URN: |
10.1007/s00253-018-9236-6 |
|---|
| Katalog-ID: |
OLC2050795327 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | OLC2050795327 | ||
| 003 | DE-627 | ||
| 005 | 20230516185735.0 | ||
| 007 | tu | ||
| 008 | 200820s2018 xx ||||| 00| ||eng c | ||
| 024 | 7 | |a 10.1007/s00253-018-9236-6 |2 doi | |
| 035 | |a (DE-627)OLC2050795327 | ||
| 035 | |a (DE-He213)s00253-018-9236-6-p | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 082 | 0 | 4 | |a 570 |q VZ |
| 084 | |a 12 |2 ssgn | ||
| 084 | |a BIODIV |q DE-30 |2 fid | ||
| 100 | 1 | |a Meng, Xiangfeng |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity |
| 264 | 1 | |c 2018 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
| 338 | |a Band |b nc |2 rdacarrier | ||
| 500 | |a © Springer-Verlag GmbH Germany, part of Springer Nature 2018 | ||
| 520 | |a Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase. | ||
| 650 | 4 | |a Branching sucrase | |
| 650 | 4 | |a Glucansucrase | |
| 650 | 4 | |a GH70 | |
| 650 | 4 | |a Glucan | |
| 700 | 1 | |a Gangoiti, Joana |4 aut | |
| 700 | 1 | |a Wang, Xiaofei |4 aut | |
| 700 | 1 | |a Grijpstra, Pieter |4 aut | |
| 700 | 1 | |a van Leeuwen, Sander S. |4 aut | |
| 700 | 1 | |a Pijning, Tjaard |4 aut | |
| 700 | 1 | |a Dijkhuizen, Lubbert |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Applied microbiology and biotechnology |d Springer Berlin Heidelberg, 1984 |g 102(2018), 18 vom: 24. Juli, Seite 7935-7950 |w (DE-627)129942634 |w (DE-600)392453-1 |w (DE-576)015507750 |x 0175-7598 |7 nnns |
| 773 | 1 | 8 | |g volume:102 |g year:2018 |g number:18 |g day:24 |g month:07 |g pages:7935-7950 |
| 856 | 4 | 1 | |u https://doi.org/10.1007/s00253-018-9236-6 |z lizenzpflichtig |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a SYSFLAG_A | ||
| 912 | |a GBV_OLC | ||
| 912 | |a FID-BIODIV | ||
| 912 | |a SSG-OLC-TEC | ||
| 912 | |a SSG-OLC-CHE | ||
| 912 | |a SSG-OLC-PHA | ||
| 912 | |a SSG-OLC-DE-84 | ||
| 912 | |a GBV_ILN_70 | ||
| 912 | |a GBV_ILN_130 | ||
| 912 | |a GBV_ILN_267 | ||
| 912 | |a GBV_ILN_2018 | ||
| 912 | |a GBV_ILN_4012 | ||
| 912 | |a GBV_ILN_4277 | ||
| 912 | |a GBV_ILN_4305 | ||
| 951 | |a AR | ||
| 952 | |d 102 |j 2018 |e 18 |b 24 |c 07 |h 7935-7950 | ||
| author_variant |
x m xm j g jg x w xw p g pg l s s v lss lssv t p tp l d ld |
|---|---|
| matchkey_str |
article:01757598:2018----::iceiacaatrztooah0rtifolcoailsukedm26wttoaayidmis |
| hierarchy_sort_str |
2018 |
| publishDate |
2018 |
| allfields |
10.1007/s00253-018-9236-6 doi (DE-627)OLC2050795327 (DE-He213)s00253-018-9236-6-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Meng, Xiangfeng verfasserin aut Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity 2018 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase. Branching sucrase Glucansucrase GH70 Glucan Gangoiti, Joana aut Wang, Xiaofei aut Grijpstra, Pieter aut van Leeuwen, Sander S. aut Pijning, Tjaard aut Dijkhuizen, Lubbert aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 102(2018), 18 vom: 24. Juli, Seite 7935-7950 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:102 year:2018 number:18 day:24 month:07 pages:7935-7950 https://doi.org/10.1007/s00253-018-9236-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_130 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4277 GBV_ILN_4305 AR 102 2018 18 24 07 7935-7950 |
| spelling |
10.1007/s00253-018-9236-6 doi (DE-627)OLC2050795327 (DE-He213)s00253-018-9236-6-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Meng, Xiangfeng verfasserin aut Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity 2018 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase. Branching sucrase Glucansucrase GH70 Glucan Gangoiti, Joana aut Wang, Xiaofei aut Grijpstra, Pieter aut van Leeuwen, Sander S. aut Pijning, Tjaard aut Dijkhuizen, Lubbert aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 102(2018), 18 vom: 24. Juli, Seite 7935-7950 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:102 year:2018 number:18 day:24 month:07 pages:7935-7950 https://doi.org/10.1007/s00253-018-9236-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_130 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4277 GBV_ILN_4305 AR 102 2018 18 24 07 7935-7950 |
| allfields_unstemmed |
10.1007/s00253-018-9236-6 doi (DE-627)OLC2050795327 (DE-He213)s00253-018-9236-6-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Meng, Xiangfeng verfasserin aut Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity 2018 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase. Branching sucrase Glucansucrase GH70 Glucan Gangoiti, Joana aut Wang, Xiaofei aut Grijpstra, Pieter aut van Leeuwen, Sander S. aut Pijning, Tjaard aut Dijkhuizen, Lubbert aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 102(2018), 18 vom: 24. Juli, Seite 7935-7950 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:102 year:2018 number:18 day:24 month:07 pages:7935-7950 https://doi.org/10.1007/s00253-018-9236-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_130 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4277 GBV_ILN_4305 AR 102 2018 18 24 07 7935-7950 |
| allfieldsGer |
10.1007/s00253-018-9236-6 doi (DE-627)OLC2050795327 (DE-He213)s00253-018-9236-6-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Meng, Xiangfeng verfasserin aut Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity 2018 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase. Branching sucrase Glucansucrase GH70 Glucan Gangoiti, Joana aut Wang, Xiaofei aut Grijpstra, Pieter aut van Leeuwen, Sander S. aut Pijning, Tjaard aut Dijkhuizen, Lubbert aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 102(2018), 18 vom: 24. Juli, Seite 7935-7950 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:102 year:2018 number:18 day:24 month:07 pages:7935-7950 https://doi.org/10.1007/s00253-018-9236-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_130 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4277 GBV_ILN_4305 AR 102 2018 18 24 07 7935-7950 |
| allfieldsSound |
10.1007/s00253-018-9236-6 doi (DE-627)OLC2050795327 (DE-He213)s00253-018-9236-6-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Meng, Xiangfeng verfasserin aut Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity 2018 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase. Branching sucrase Glucansucrase GH70 Glucan Gangoiti, Joana aut Wang, Xiaofei aut Grijpstra, Pieter aut van Leeuwen, Sander S. aut Pijning, Tjaard aut Dijkhuizen, Lubbert aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 102(2018), 18 vom: 24. Juli, Seite 7935-7950 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:102 year:2018 number:18 day:24 month:07 pages:7935-7950 https://doi.org/10.1007/s00253-018-9236-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_130 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4277 GBV_ILN_4305 AR 102 2018 18 24 07 7935-7950 |
| language |
English |
| source |
Enthalten in Applied microbiology and biotechnology 102(2018), 18 vom: 24. Juli, Seite 7935-7950 volume:102 year:2018 number:18 day:24 month:07 pages:7935-7950 |
| sourceStr |
Enthalten in Applied microbiology and biotechnology 102(2018), 18 vom: 24. Juli, Seite 7935-7950 volume:102 year:2018 number:18 day:24 month:07 pages:7935-7950 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| topic_facet |
Branching sucrase Glucansucrase GH70 Glucan |
| dewey-raw |
570 |
| isfreeaccess_bool |
false |
| container_title |
Applied microbiology and biotechnology |
| authorswithroles_txt_mv |
Meng, Xiangfeng @@aut@@ Gangoiti, Joana @@aut@@ Wang, Xiaofei @@aut@@ Grijpstra, Pieter @@aut@@ van Leeuwen, Sander S. @@aut@@ Pijning, Tjaard @@aut@@ Dijkhuizen, Lubbert @@aut@@ |
| publishDateDaySort_date |
2018-07-24T00:00:00Z |
| hierarchy_top_id |
129942634 |
| dewey-sort |
3570 |
| id |
OLC2050795327 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">OLC2050795327</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230516185735.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">200820s2018 xx ||||| 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s00253-018-9236-6</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC2050795327</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-He213)s00253-018-9236-6-p</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">12</subfield><subfield code="2">ssgn</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">BIODIV</subfield><subfield code="q">DE-30</subfield><subfield code="2">fid</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Meng, Xiangfeng</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2018</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Springer-Verlag GmbH Germany, part of Springer Nature 2018</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Branching sucrase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Glucansucrase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">GH70</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Glucan</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gangoiti, Joana</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Xiaofei</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Grijpstra, Pieter</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">van Leeuwen, Sander S.</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pijning, Tjaard</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Dijkhuizen, Lubbert</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Applied microbiology and biotechnology</subfield><subfield code="d">Springer Berlin Heidelberg, 1984</subfield><subfield code="g">102(2018), 18 vom: 24. Juli, Seite 7935-7950</subfield><subfield code="w">(DE-627)129942634</subfield><subfield code="w">(DE-600)392453-1</subfield><subfield code="w">(DE-576)015507750</subfield><subfield code="x">0175-7598</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:102</subfield><subfield code="g">year:2018</subfield><subfield code="g">number:18</subfield><subfield code="g">day:24</subfield><subfield code="g">month:07</subfield><subfield code="g">pages:7935-7950</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">https://doi.org/10.1007/s00253-018-9236-6</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-TEC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_130</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_267</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2018</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4277</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">102</subfield><subfield code="j">2018</subfield><subfield code="e">18</subfield><subfield code="b">24</subfield><subfield code="c">07</subfield><subfield code="h">7935-7950</subfield></datafield></record></collection>
|
| author |
Meng, Xiangfeng |
| spellingShingle |
Meng, Xiangfeng ddc 570 ssgn 12 fid BIODIV misc Branching sucrase misc Glucansucrase misc GH70 misc Glucan Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity |
| authorStr |
Meng, Xiangfeng |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)129942634 |
| format |
Article |
| dewey-ones |
570 - Life sciences; biology |
| delete_txt_mv |
keep |
| author_role |
aut aut aut aut aut aut aut |
| collection |
OLC |
| remote_str |
false |
| illustrated |
Not Illustrated |
| issn |
0175-7598 |
| topic_title |
570 VZ 12 ssgn BIODIV DE-30 fid Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity Branching sucrase Glucansucrase GH70 Glucan |
| topic |
ddc 570 ssgn 12 fid BIODIV misc Branching sucrase misc Glucansucrase misc GH70 misc Glucan |
| topic_unstemmed |
ddc 570 ssgn 12 fid BIODIV misc Branching sucrase misc Glucansucrase misc GH70 misc Glucan |
| topic_browse |
ddc 570 ssgn 12 fid BIODIV misc Branching sucrase misc Glucansucrase misc GH70 misc Glucan |
| format_facet |
Aufsätze Gedruckte Aufsätze |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
nc |
| hierarchy_parent_title |
Applied microbiology and biotechnology |
| hierarchy_parent_id |
129942634 |
| dewey-tens |
570 - Life sciences; biology |
| hierarchy_top_title |
Applied microbiology and biotechnology |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 |
| title |
Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity |
| ctrlnum |
(DE-627)OLC2050795327 (DE-He213)s00253-018-9236-6-p |
| title_full |
Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity |
| author_sort |
Meng, Xiangfeng |
| journal |
Applied microbiology and biotechnology |
| journalStr |
Applied microbiology and biotechnology |
| lang_code |
eng |
| isOA_bool |
false |
| dewey-hundreds |
500 - Science |
| recordtype |
marc |
| publishDateSort |
2018 |
| contenttype_str_mv |
txt |
| container_start_page |
7935 |
| author_browse |
Meng, Xiangfeng Gangoiti, Joana Wang, Xiaofei Grijpstra, Pieter van Leeuwen, Sander S. Pijning, Tjaard Dijkhuizen, Lubbert |
| container_volume |
102 |
| class |
570 VZ 12 ssgn BIODIV DE-30 fid |
| format_se |
Aufsätze |
| author-letter |
Meng, Xiangfeng |
| doi_str_mv |
10.1007/s00253-018-9236-6 |
| dewey-full |
570 |
| title_sort |
biochemical characterization of a gh70 protein from lactobacillus kunkeei dsm 12361 with two catalytic domains involving branching sucrase activity |
| title_auth |
Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity |
| abstract |
Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase. © Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
| abstractGer |
Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase. © Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
| abstract_unstemmed |
Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase. © Springer-Verlag GmbH Germany, part of Springer Nature 2018 |
| collection_details |
GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_130 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4277 GBV_ILN_4305 |
| container_issue |
18 |
| title_short |
Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity |
| url |
https://doi.org/10.1007/s00253-018-9236-6 |
| remote_bool |
false |
| author2 |
Gangoiti, Joana Wang, Xiaofei Grijpstra, Pieter van Leeuwen, Sander S. Pijning, Tjaard Dijkhuizen, Lubbert |
| author2Str |
Gangoiti, Joana Wang, Xiaofei Grijpstra, Pieter van Leeuwen, Sander S. Pijning, Tjaard Dijkhuizen, Lubbert |
| ppnlink |
129942634 |
| mediatype_str_mv |
n |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| doi_str |
10.1007/s00253-018-9236-6 |
| up_date |
2024-07-04T02:54:13.620Z |
| _version_ |
1803615368507293696 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">OLC2050795327</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230516185735.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">200820s2018 xx ||||| 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s00253-018-9236-6</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC2050795327</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-He213)s00253-018-9236-6-p</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">12</subfield><subfield code="2">ssgn</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">BIODIV</subfield><subfield code="q">DE-30</subfield><subfield code="2">fid</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Meng, Xiangfeng</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Biochemical characterization of a GH70 protein from Lactobacillus kunkeei DSM 12361 with two catalytic domains involving branching sucrase activity</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2018</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Springer-Verlag GmbH Germany, part of Springer Nature 2018</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract The fructophilic bacterium Lactobacillus kunkeei has promising applications as probiotics promoting the health of both honey bees and humans. Here, we report the synthesis of a highly branched dextran by L. kunkeei DSM 12361 and biochemical characterization of a GH70 enzyme (GtfZ). Sequence analysis revealed that GtfZ harbors two separate catalytic cores (CD1 and CD2), predicted to have glucansucrase and branching sucrase specificity, respectively. GtfZ-CD1 was not characterized biochemically due to its unsuccessful expression. With only sucrose as substrate, GtfZ-CD2 was found to mainly catalyze sucrose hydrolysis and leucrose synthesis. When dextran was available as acceptor substrate, GtfZ-CD2 displayed an efficient transglycosidase activity with sucrose as donor substrate. Kinetic analysis showed that the GtfZ-CD2-catalyzed transglycosylation reaction follows a Ping Pong Bi Bi mechanism, indicating the in-turn binding of donor and acceptor substrates in the active site. Structural characterization of the products revealed that GtfZ-CD2 catalyzes the synthesis of single glucosyl (α1 → 3) linked branches onto dextran, resulting in the production of highly branched comb-like α-glucan products. These (α1 → 3) branches can be formed on adjacent positions, as shown when isomaltotriose was used as acceptor substrate. Homology modeling of the GtfZ-CD1 and GtfZ-CD2 protein structure strongly suggests that amino acid differences in conserved motifs II, III, and IV in the catalytic domain contribute to product specificity. Our present study highlights the ability of beneficial lactic acid bacteria to produce structurally complex α-glucans and provides novel insights into the molecular mechanism of an (α1 → 3) branching sucrase.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Branching sucrase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Glucansucrase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">GH70</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Glucan</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gangoiti, Joana</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Xiaofei</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Grijpstra, Pieter</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">van Leeuwen, Sander S.</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pijning, Tjaard</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Dijkhuizen, Lubbert</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Applied microbiology and biotechnology</subfield><subfield code="d">Springer Berlin Heidelberg, 1984</subfield><subfield code="g">102(2018), 18 vom: 24. Juli, Seite 7935-7950</subfield><subfield code="w">(DE-627)129942634</subfield><subfield code="w">(DE-600)392453-1</subfield><subfield code="w">(DE-576)015507750</subfield><subfield code="x">0175-7598</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:102</subfield><subfield code="g">year:2018</subfield><subfield code="g">number:18</subfield><subfield code="g">day:24</subfield><subfield code="g">month:07</subfield><subfield code="g">pages:7935-7950</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">https://doi.org/10.1007/s00253-018-9236-6</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-TEC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_130</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_267</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2018</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4277</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">102</subfield><subfield code="j">2018</subfield><subfield code="e">18</subfield><subfield code="b">24</subfield><subfield code="c">07</subfield><subfield code="h">7935-7950</subfield></datafield></record></collection>
|
| score |
7.400879 |