Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition
Exopolysaccharides produced by lactic acid bacteria are extensively used for food applications. Glucansucrase enzymes of lactic acid bacteria use sucrose to catalyze the synthesis of α-glucans with different linkage compositions, size and physico-chemical properties. Crystallographic studies of GTF1...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Meng, Xiangfeng [verfasserIn] |
|---|
| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Rechteinformationen: |
Nutzungsrecht: Copyright © 2016 Elsevier Ltd. All rights reserved. |
|---|
| Übergeordnetes Werk: |
Enthalten in: Food chemistry - Amsterdam [u.a.] : Elsevier, 1976, 217(2017), Seite 81-90 |
|---|---|
| Übergeordnetes Werk: |
volume:217 ; year:2017 ; pages:81-90 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.foodchem.2016.08.087 |
|---|
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OLC1987497635 |
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| 520 | |a Exopolysaccharides produced by lactic acid bacteria are extensively used for food applications. Glucansucrase enzymes of lactic acid bacteria use sucrose to catalyze the synthesis of α-glucans with different linkage compositions, size and physico-chemical properties. Crystallographic studies of GTF180-ΔN show that at the acceptor binding sites +1 and +2, residue W1065 provides stacking interactions to the glucosyl moiety. However, the detailed functional roles of W1065 have not been elucidated. We performed random mutagenesis targeting residue W1065 of GTF180-ΔN, resulting in the generation of 10 mutant enzymes that were characterized regarding activity and product specificity. Characterization of mutant enzymes showed that residue W1065 is critical for the activity of GTF180-ΔN. Using sucrose, and sucrose (donor) plus maltose (acceptor) as substrates, the mutant enzymes synthesized polysaccharides and oligosaccharides with changed linkage composition. The stacking interaction of an aromatic residue at position 1065 is essential for polysaccharide synthesis. | ||
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10.1016/j.foodchem.2016.08.087 doi PQ20170721 (DE-627)OLC1987497635 (DE-599)GBVOLC1987497635 (PRQ)c1667-8c045340314837670c5c47b7edd8063ffe3a5ef3127c2ea6ae7147c11d49e7b30 (KEY)0039580320170000217000000081characterizationoftheglucansucrasegtf180w1065mutan DE-627 ger DE-627 rakwb eng 540 660 DE-600 58.34 bkl 58.00 bkl Meng, Xiangfeng verfasserin aut Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Exopolysaccharides produced by lactic acid bacteria are extensively used for food applications. Glucansucrase enzymes of lactic acid bacteria use sucrose to catalyze the synthesis of α-glucans with different linkage compositions, size and physico-chemical properties. Crystallographic studies of GTF180-ΔN show that at the acceptor binding sites +1 and +2, residue W1065 provides stacking interactions to the glucosyl moiety. However, the detailed functional roles of W1065 have not been elucidated. We performed random mutagenesis targeting residue W1065 of GTF180-ΔN, resulting in the generation of 10 mutant enzymes that were characterized regarding activity and product specificity. Characterization of mutant enzymes showed that residue W1065 is critical for the activity of GTF180-ΔN. Using sucrose, and sucrose (donor) plus maltose (acceptor) as substrates, the mutant enzymes synthesized polysaccharides and oligosaccharides with changed linkage composition. The stacking interaction of an aromatic residue at position 1065 is essential for polysaccharide synthesis. Nutzungsrecht: Copyright © 2016 Elsevier Ltd. All rights reserved. Pijning, Tjaard oth Tietema, Martin oth Dobruchowska, Justyna M oth Yin, Huifang oth Gerwig, Gerrit J oth Kralj, Slavko oth Dijkhuizen, Lubbert oth Enthalten in Food chemistry Amsterdam [u.a.] : Elsevier, 1976 217(2017), Seite 81-90 (DE-627)129611751 (DE-600)243123-3 (DE-576)015107418 0308-8146 nnns volume:217 year:2017 pages:81-90 http://dx.doi.org/10.1016/j.foodchem.2016.08.087 Volltext http://www.ncbi.nlm.nih.gov/pubmed/27664611 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4219 58.34 AVZ 58.00 AVZ AR 217 2017 81-90 |
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10.1016/j.foodchem.2016.08.087 doi PQ20170721 (DE-627)OLC1987497635 (DE-599)GBVOLC1987497635 (PRQ)c1667-8c045340314837670c5c47b7edd8063ffe3a5ef3127c2ea6ae7147c11d49e7b30 (KEY)0039580320170000217000000081characterizationoftheglucansucrasegtf180w1065mutan DE-627 ger DE-627 rakwb eng 540 660 DE-600 58.34 bkl 58.00 bkl Meng, Xiangfeng verfasserin aut Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Exopolysaccharides produced by lactic acid bacteria are extensively used for food applications. Glucansucrase enzymes of lactic acid bacteria use sucrose to catalyze the synthesis of α-glucans with different linkage compositions, size and physico-chemical properties. Crystallographic studies of GTF180-ΔN show that at the acceptor binding sites +1 and +2, residue W1065 provides stacking interactions to the glucosyl moiety. However, the detailed functional roles of W1065 have not been elucidated. We performed random mutagenesis targeting residue W1065 of GTF180-ΔN, resulting in the generation of 10 mutant enzymes that were characterized regarding activity and product specificity. Characterization of mutant enzymes showed that residue W1065 is critical for the activity of GTF180-ΔN. Using sucrose, and sucrose (donor) plus maltose (acceptor) as substrates, the mutant enzymes synthesized polysaccharides and oligosaccharides with changed linkage composition. The stacking interaction of an aromatic residue at position 1065 is essential for polysaccharide synthesis. Nutzungsrecht: Copyright © 2016 Elsevier Ltd. All rights reserved. Pijning, Tjaard oth Tietema, Martin oth Dobruchowska, Justyna M oth Yin, Huifang oth Gerwig, Gerrit J oth Kralj, Slavko oth Dijkhuizen, Lubbert oth Enthalten in Food chemistry Amsterdam [u.a.] : Elsevier, 1976 217(2017), Seite 81-90 (DE-627)129611751 (DE-600)243123-3 (DE-576)015107418 0308-8146 nnns volume:217 year:2017 pages:81-90 http://dx.doi.org/10.1016/j.foodchem.2016.08.087 Volltext http://www.ncbi.nlm.nih.gov/pubmed/27664611 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4219 58.34 AVZ 58.00 AVZ AR 217 2017 81-90 |
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10.1016/j.foodchem.2016.08.087 doi PQ20170721 (DE-627)OLC1987497635 (DE-599)GBVOLC1987497635 (PRQ)c1667-8c045340314837670c5c47b7edd8063ffe3a5ef3127c2ea6ae7147c11d49e7b30 (KEY)0039580320170000217000000081characterizationoftheglucansucrasegtf180w1065mutan DE-627 ger DE-627 rakwb eng 540 660 DE-600 58.34 bkl 58.00 bkl Meng, Xiangfeng verfasserin aut Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Exopolysaccharides produced by lactic acid bacteria are extensively used for food applications. Glucansucrase enzymes of lactic acid bacteria use sucrose to catalyze the synthesis of α-glucans with different linkage compositions, size and physico-chemical properties. Crystallographic studies of GTF180-ΔN show that at the acceptor binding sites +1 and +2, residue W1065 provides stacking interactions to the glucosyl moiety. However, the detailed functional roles of W1065 have not been elucidated. We performed random mutagenesis targeting residue W1065 of GTF180-ΔN, resulting in the generation of 10 mutant enzymes that were characterized regarding activity and product specificity. Characterization of mutant enzymes showed that residue W1065 is critical for the activity of GTF180-ΔN. Using sucrose, and sucrose (donor) plus maltose (acceptor) as substrates, the mutant enzymes synthesized polysaccharides and oligosaccharides with changed linkage composition. The stacking interaction of an aromatic residue at position 1065 is essential for polysaccharide synthesis. Nutzungsrecht: Copyright © 2016 Elsevier Ltd. All rights reserved. Pijning, Tjaard oth Tietema, Martin oth Dobruchowska, Justyna M oth Yin, Huifang oth Gerwig, Gerrit J oth Kralj, Slavko oth Dijkhuizen, Lubbert oth Enthalten in Food chemistry Amsterdam [u.a.] : Elsevier, 1976 217(2017), Seite 81-90 (DE-627)129611751 (DE-600)243123-3 (DE-576)015107418 0308-8146 nnns volume:217 year:2017 pages:81-90 http://dx.doi.org/10.1016/j.foodchem.2016.08.087 Volltext http://www.ncbi.nlm.nih.gov/pubmed/27664611 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4219 58.34 AVZ 58.00 AVZ AR 217 2017 81-90 |
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10.1016/j.foodchem.2016.08.087 doi PQ20170721 (DE-627)OLC1987497635 (DE-599)GBVOLC1987497635 (PRQ)c1667-8c045340314837670c5c47b7edd8063ffe3a5ef3127c2ea6ae7147c11d49e7b30 (KEY)0039580320170000217000000081characterizationoftheglucansucrasegtf180w1065mutan DE-627 ger DE-627 rakwb eng 540 660 DE-600 58.34 bkl 58.00 bkl Meng, Xiangfeng verfasserin aut Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Exopolysaccharides produced by lactic acid bacteria are extensively used for food applications. Glucansucrase enzymes of lactic acid bacteria use sucrose to catalyze the synthesis of α-glucans with different linkage compositions, size and physico-chemical properties. Crystallographic studies of GTF180-ΔN show that at the acceptor binding sites +1 and +2, residue W1065 provides stacking interactions to the glucosyl moiety. However, the detailed functional roles of W1065 have not been elucidated. We performed random mutagenesis targeting residue W1065 of GTF180-ΔN, resulting in the generation of 10 mutant enzymes that were characterized regarding activity and product specificity. Characterization of mutant enzymes showed that residue W1065 is critical for the activity of GTF180-ΔN. Using sucrose, and sucrose (donor) plus maltose (acceptor) as substrates, the mutant enzymes synthesized polysaccharides and oligosaccharides with changed linkage composition. The stacking interaction of an aromatic residue at position 1065 is essential for polysaccharide synthesis. Nutzungsrecht: Copyright © 2016 Elsevier Ltd. All rights reserved. Pijning, Tjaard oth Tietema, Martin oth Dobruchowska, Justyna M oth Yin, Huifang oth Gerwig, Gerrit J oth Kralj, Slavko oth Dijkhuizen, Lubbert oth Enthalten in Food chemistry Amsterdam [u.a.] : Elsevier, 1976 217(2017), Seite 81-90 (DE-627)129611751 (DE-600)243123-3 (DE-576)015107418 0308-8146 nnns volume:217 year:2017 pages:81-90 http://dx.doi.org/10.1016/j.foodchem.2016.08.087 Volltext http://www.ncbi.nlm.nih.gov/pubmed/27664611 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4219 58.34 AVZ 58.00 AVZ AR 217 2017 81-90 |
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10.1016/j.foodchem.2016.08.087 doi PQ20170721 (DE-627)OLC1987497635 (DE-599)GBVOLC1987497635 (PRQ)c1667-8c045340314837670c5c47b7edd8063ffe3a5ef3127c2ea6ae7147c11d49e7b30 (KEY)0039580320170000217000000081characterizationoftheglucansucrasegtf180w1065mutan DE-627 ger DE-627 rakwb eng 540 660 DE-600 58.34 bkl 58.00 bkl Meng, Xiangfeng verfasserin aut Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Exopolysaccharides produced by lactic acid bacteria are extensively used for food applications. Glucansucrase enzymes of lactic acid bacteria use sucrose to catalyze the synthesis of α-glucans with different linkage compositions, size and physico-chemical properties. Crystallographic studies of GTF180-ΔN show that at the acceptor binding sites +1 and +2, residue W1065 provides stacking interactions to the glucosyl moiety. However, the detailed functional roles of W1065 have not been elucidated. We performed random mutagenesis targeting residue W1065 of GTF180-ΔN, resulting in the generation of 10 mutant enzymes that were characterized regarding activity and product specificity. Characterization of mutant enzymes showed that residue W1065 is critical for the activity of GTF180-ΔN. Using sucrose, and sucrose (donor) plus maltose (acceptor) as substrates, the mutant enzymes synthesized polysaccharides and oligosaccharides with changed linkage composition. The stacking interaction of an aromatic residue at position 1065 is essential for polysaccharide synthesis. Nutzungsrecht: Copyright © 2016 Elsevier Ltd. All rights reserved. Pijning, Tjaard oth Tietema, Martin oth Dobruchowska, Justyna M oth Yin, Huifang oth Gerwig, Gerrit J oth Kralj, Slavko oth Dijkhuizen, Lubbert oth Enthalten in Food chemistry Amsterdam [u.a.] : Elsevier, 1976 217(2017), Seite 81-90 (DE-627)129611751 (DE-600)243123-3 (DE-576)015107418 0308-8146 nnns volume:217 year:2017 pages:81-90 http://dx.doi.org/10.1016/j.foodchem.2016.08.087 Volltext http://www.ncbi.nlm.nih.gov/pubmed/27664611 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_4219 58.34 AVZ 58.00 AVZ AR 217 2017 81-90 |
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Meng, Xiangfeng |
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Meng, Xiangfeng ddc 540 bkl 58.34 bkl 58.00 Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition |
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540 660 DE-600 58.34 bkl 58.00 bkl Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition |
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Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition |
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Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition |
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characterization of the glucansucrase gtf180 w1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition |
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Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition |
| abstract |
Exopolysaccharides produced by lactic acid bacteria are extensively used for food applications. Glucansucrase enzymes of lactic acid bacteria use sucrose to catalyze the synthesis of α-glucans with different linkage compositions, size and physico-chemical properties. Crystallographic studies of GTF180-ΔN show that at the acceptor binding sites +1 and +2, residue W1065 provides stacking interactions to the glucosyl moiety. However, the detailed functional roles of W1065 have not been elucidated. We performed random mutagenesis targeting residue W1065 of GTF180-ΔN, resulting in the generation of 10 mutant enzymes that were characterized regarding activity and product specificity. Characterization of mutant enzymes showed that residue W1065 is critical for the activity of GTF180-ΔN. Using sucrose, and sucrose (donor) plus maltose (acceptor) as substrates, the mutant enzymes synthesized polysaccharides and oligosaccharides with changed linkage composition. The stacking interaction of an aromatic residue at position 1065 is essential for polysaccharide synthesis. |
| abstractGer |
Exopolysaccharides produced by lactic acid bacteria are extensively used for food applications. Glucansucrase enzymes of lactic acid bacteria use sucrose to catalyze the synthesis of α-glucans with different linkage compositions, size and physico-chemical properties. Crystallographic studies of GTF180-ΔN show that at the acceptor binding sites +1 and +2, residue W1065 provides stacking interactions to the glucosyl moiety. However, the detailed functional roles of W1065 have not been elucidated. We performed random mutagenesis targeting residue W1065 of GTF180-ΔN, resulting in the generation of 10 mutant enzymes that were characterized regarding activity and product specificity. Characterization of mutant enzymes showed that residue W1065 is critical for the activity of GTF180-ΔN. Using sucrose, and sucrose (donor) plus maltose (acceptor) as substrates, the mutant enzymes synthesized polysaccharides and oligosaccharides with changed linkage composition. The stacking interaction of an aromatic residue at position 1065 is essential for polysaccharide synthesis. |
| abstract_unstemmed |
Exopolysaccharides produced by lactic acid bacteria are extensively used for food applications. Glucansucrase enzymes of lactic acid bacteria use sucrose to catalyze the synthesis of α-glucans with different linkage compositions, size and physico-chemical properties. Crystallographic studies of GTF180-ΔN show that at the acceptor binding sites +1 and +2, residue W1065 provides stacking interactions to the glucosyl moiety. However, the detailed functional roles of W1065 have not been elucidated. We performed random mutagenesis targeting residue W1065 of GTF180-ΔN, resulting in the generation of 10 mutant enzymes that were characterized regarding activity and product specificity. Characterization of mutant enzymes showed that residue W1065 is critical for the activity of GTF180-ΔN. Using sucrose, and sucrose (donor) plus maltose (acceptor) as substrates, the mutant enzymes synthesized polysaccharides and oligosaccharides with changed linkage composition. The stacking interaction of an aromatic residue at position 1065 is essential for polysaccharide synthesis. |
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Characterization of the glucansucrase GTF180 W1065 mutant enzymes producing polysaccharides and oligosaccharides with altered linkage composition |
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http://dx.doi.org/10.1016/j.foodchem.2016.08.087 http://www.ncbi.nlm.nih.gov/pubmed/27664611 |
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Pijning, Tjaard Tietema, Martin Dobruchowska, Justyna M Yin, Huifang Gerwig, Gerrit J Kralj, Slavko Dijkhuizen, Lubbert |
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