Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6
Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 f...
Ausführliche Beschreibung
Autor*in: |
Chaabouni, Semia Ellouz [verfasserIn] |
---|
Format: |
Artikel |
---|---|
Sprache: |
Englisch |
Erschienen: |
2005 |
---|
Anmerkung: |
© Humana Press Inc 2005 |
---|
Übergeordnetes Werk: |
Enthalten in: Applied biochemistry and biotechnology / A - Humana Press, 1994, 125(2005), 2 vom: Mai, Seite 99-112 |
---|---|
Übergeordnetes Werk: |
volume:125 ; year:2005 ; number:2 ; month:05 ; pages:99-112 |
Links: |
---|
DOI / URN: |
10.1385/ABAB:125:2:099 |
---|
Katalog-ID: |
OLC2130512496 |
---|
LEADER | 01000naa a22002652 4500 | ||
---|---|---|---|
001 | OLC2130512496 | ||
003 | DE-627 | ||
005 | 20230506021542.0 | ||
007 | tu | ||
008 | 230506s2005 xx ||||| 00| ||eng c | ||
024 | 7 | |a 10.1385/ABAB:125:2:099 |2 doi | |
035 | |a (DE-627)OLC2130512496 | ||
035 | |a (DE-He213)ABAB:125:2:099-p | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
041 | |a eng | ||
082 | 0 | 4 | |a 570 |a 540 |a 660 |q VZ |
084 | |a 12 |2 ssgn | ||
084 | |a 42.00 |2 bkl | ||
100 | 1 | |a Chaabouni, Semia Ellouz |e verfasserin |4 aut | |
245 | 1 | 0 | |a Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 |
264 | 1 | |c 2005 | |
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 © Humana Press Inc 2005 | ||
520 | |a Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $. | ||
700 | 1 | |a Mechichi, Tahar |4 aut | |
700 | 1 | |a Limam, Ferid |4 aut | |
700 | 1 | |a Marzouki, Nejib |4 aut | |
773 | 0 | 8 | |i Enthalten in |t Applied biochemistry and biotechnology / A |d Humana Press, 1994 |g 125(2005), 2 vom: Mai, Seite 99-112 |w (DE-627)182278573 |w (DE-600)1193054-8 |w (DE-576)043085105 |x 0273-2289 |7 nnns |
773 | 1 | 8 | |g volume:125 |g year:2005 |g number:2 |g month:05 |g pages:99-112 |
856 | 4 | 1 | |u https://doi.org/10.1385/ABAB:125:2:099 |z lizenzpflichtig |3 Volltext |
912 | |a GBV_USEFLAG_A | ||
912 | |a SYSFLAG_A | ||
912 | |a GBV_OLC | ||
912 | |a SSG-OLC-TEC | ||
912 | |a SSG-OLC-CHE | ||
912 | |a GBV_ILN_21 | ||
912 | |a GBV_ILN_40 | ||
912 | |a GBV_ILN_65 | ||
912 | |a GBV_ILN_70 | ||
912 | |a GBV_ILN_105 | ||
912 | |a GBV_ILN_4012 | ||
912 | |a GBV_ILN_4219 | ||
912 | |a GBV_ILN_4310 | ||
936 | b | k | |a 42.00 |q VZ |
951 | |a AR | ||
952 | |d 125 |j 2005 |e 2 |c 05 |h 99-112 |
author_variant |
s e c se sec t m tm f l fl n m nm |
---|---|
matchkey_str |
article:02732289:2005----::uiiainncaatrztootoomlclregtnolcnssrdcdye |
hierarchy_sort_str |
2005 |
bklnumber |
42.00 |
publishDate |
2005 |
allfields |
10.1385/ABAB:125:2:099 doi (DE-627)OLC2130512496 (DE-He213)ABAB:125:2:099-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Chaabouni, Semia Ellouz verfasserin aut Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Humana Press Inc 2005 Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $. Mechichi, Tahar aut Limam, Ferid aut Marzouki, Nejib aut Enthalten in Applied biochemistry and biotechnology / A Humana Press, 1994 125(2005), 2 vom: Mai, Seite 99-112 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:125 year:2005 number:2 month:05 pages:99-112 https://doi.org/10.1385/ABAB:125:2:099 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_105 GBV_ILN_4012 GBV_ILN_4219 GBV_ILN_4310 42.00 VZ AR 125 2005 2 05 99-112 |
spelling |
10.1385/ABAB:125:2:099 doi (DE-627)OLC2130512496 (DE-He213)ABAB:125:2:099-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Chaabouni, Semia Ellouz verfasserin aut Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Humana Press Inc 2005 Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $. Mechichi, Tahar aut Limam, Ferid aut Marzouki, Nejib aut Enthalten in Applied biochemistry and biotechnology / A Humana Press, 1994 125(2005), 2 vom: Mai, Seite 99-112 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:125 year:2005 number:2 month:05 pages:99-112 https://doi.org/10.1385/ABAB:125:2:099 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_105 GBV_ILN_4012 GBV_ILN_4219 GBV_ILN_4310 42.00 VZ AR 125 2005 2 05 99-112 |
allfields_unstemmed |
10.1385/ABAB:125:2:099 doi (DE-627)OLC2130512496 (DE-He213)ABAB:125:2:099-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Chaabouni, Semia Ellouz verfasserin aut Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Humana Press Inc 2005 Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $. Mechichi, Tahar aut Limam, Ferid aut Marzouki, Nejib aut Enthalten in Applied biochemistry and biotechnology / A Humana Press, 1994 125(2005), 2 vom: Mai, Seite 99-112 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:125 year:2005 number:2 month:05 pages:99-112 https://doi.org/10.1385/ABAB:125:2:099 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_105 GBV_ILN_4012 GBV_ILN_4219 GBV_ILN_4310 42.00 VZ AR 125 2005 2 05 99-112 |
allfieldsGer |
10.1385/ABAB:125:2:099 doi (DE-627)OLC2130512496 (DE-He213)ABAB:125:2:099-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Chaabouni, Semia Ellouz verfasserin aut Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Humana Press Inc 2005 Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $. Mechichi, Tahar aut Limam, Ferid aut Marzouki, Nejib aut Enthalten in Applied biochemistry and biotechnology / A Humana Press, 1994 125(2005), 2 vom: Mai, Seite 99-112 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:125 year:2005 number:2 month:05 pages:99-112 https://doi.org/10.1385/ABAB:125:2:099 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_105 GBV_ILN_4012 GBV_ILN_4219 GBV_ILN_4310 42.00 VZ AR 125 2005 2 05 99-112 |
allfieldsSound |
10.1385/ABAB:125:2:099 doi (DE-627)OLC2130512496 (DE-He213)ABAB:125:2:099-p DE-627 ger DE-627 rakwb eng 570 540 660 VZ 12 ssgn 42.00 bkl Chaabouni, Semia Ellouz verfasserin aut Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Humana Press Inc 2005 Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $. Mechichi, Tahar aut Limam, Ferid aut Marzouki, Nejib aut Enthalten in Applied biochemistry and biotechnology / A Humana Press, 1994 125(2005), 2 vom: Mai, Seite 99-112 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:125 year:2005 number:2 month:05 pages:99-112 https://doi.org/10.1385/ABAB:125:2:099 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_105 GBV_ILN_4012 GBV_ILN_4219 GBV_ILN_4310 42.00 VZ AR 125 2005 2 05 99-112 |
language |
English |
source |
Enthalten in Applied biochemistry and biotechnology / A 125(2005), 2 vom: Mai, Seite 99-112 volume:125 year:2005 number:2 month:05 pages:99-112 |
sourceStr |
Enthalten in Applied biochemistry and biotechnology / A 125(2005), 2 vom: Mai, Seite 99-112 volume:125 year:2005 number:2 month:05 pages:99-112 |
format_phy_str_mv |
Article |
institution |
findex.gbv.de |
dewey-raw |
570 |
isfreeaccess_bool |
false |
container_title |
Applied biochemistry and biotechnology / A |
authorswithroles_txt_mv |
Chaabouni, Semia Ellouz @@aut@@ Mechichi, Tahar @@aut@@ Limam, Ferid @@aut@@ Marzouki, Nejib @@aut@@ |
publishDateDaySort_date |
2005-05-01T00:00:00Z |
hierarchy_top_id |
182278573 |
dewey-sort |
3570 |
id |
OLC2130512496 |
language_de |
englisch |
fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">OLC2130512496</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506021542.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">230506s2005 xx ||||| 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1385/ABAB:125:2:099</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC2130512496</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-He213)ABAB:125:2:099-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="a">540</subfield><subfield code="a">660</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">42.00</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Chaabouni, Semia Ellouz</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2005</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">© Humana Press Inc 2005</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Mechichi, Tahar</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Limam, Ferid</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Marzouki, Nejib</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Applied biochemistry and biotechnology / A</subfield><subfield code="d">Humana Press, 1994</subfield><subfield code="g">125(2005), 2 vom: Mai, Seite 99-112</subfield><subfield code="w">(DE-627)182278573</subfield><subfield code="w">(DE-600)1193054-8</subfield><subfield code="w">(DE-576)043085105</subfield><subfield code="x">0273-2289</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:125</subfield><subfield code="g">year:2005</subfield><subfield code="g">number:2</subfield><subfield code="g">month:05</subfield><subfield code="g">pages:99-112</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">https://doi.org/10.1385/ABAB:125:2:099</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">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">GBV_ILN_21</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_65</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_105</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_4219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4310</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">42.00</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">125</subfield><subfield code="j">2005</subfield><subfield code="e">2</subfield><subfield code="c">05</subfield><subfield code="h">99-112</subfield></datafield></record></collection>
|
author |
Chaabouni, Semia Ellouz |
spellingShingle |
Chaabouni, Semia Ellouz ddc 570 ssgn 12 bkl 42.00 Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 |
authorStr |
Chaabouni, Semia Ellouz |
ppnlink_with_tag_str_mv |
@@773@@(DE-627)182278573 |
format |
Article |
dewey-ones |
570 - Life sciences; biology 540 - Chemistry & allied sciences 660 - Chemical engineering |
delete_txt_mv |
keep |
author_role |
aut aut aut aut |
collection |
OLC |
remote_str |
false |
illustrated |
Not Illustrated |
issn |
0273-2289 |
topic_title |
570 540 660 VZ 12 ssgn 42.00 bkl Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 |
topic |
ddc 570 ssgn 12 bkl 42.00 |
topic_unstemmed |
ddc 570 ssgn 12 bkl 42.00 |
topic_browse |
ddc 570 ssgn 12 bkl 42.00 |
format_facet |
Aufsätze Gedruckte Aufsätze |
format_main_str_mv |
Text Zeitschrift/Artikel |
carriertype_str_mv |
nc |
hierarchy_parent_title |
Applied biochemistry and biotechnology / A |
hierarchy_parent_id |
182278573 |
dewey-tens |
570 - Life sciences; biology 540 - Chemistry 660 - Chemical engineering |
hierarchy_top_title |
Applied biochemistry and biotechnology / A |
isfreeaccess_txt |
false |
familylinks_str_mv |
(DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 |
title |
Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 |
ctrlnum |
(DE-627)OLC2130512496 (DE-He213)ABAB:125:2:099-p |
title_full |
Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 |
author_sort |
Chaabouni, Semia Ellouz |
journal |
Applied biochemistry and biotechnology / A |
journalStr |
Applied biochemistry and biotechnology / A |
lang_code |
eng |
isOA_bool |
false |
dewey-hundreds |
500 - Science 600 - Technology |
recordtype |
marc |
publishDateSort |
2005 |
contenttype_str_mv |
txt |
container_start_page |
99 |
author_browse |
Chaabouni, Semia Ellouz Mechichi, Tahar Limam, Ferid Marzouki, Nejib |
container_volume |
125 |
class |
570 540 660 VZ 12 ssgn 42.00 bkl |
format_se |
Aufsätze |
author-letter |
Chaabouni, Semia Ellouz |
doi_str_mv |
10.1385/ABAB:125:2:099 |
dewey-full |
570 540 660 |
title_sort |
purification and characterization of two low molecular weight endoglucanases produced by penicillium occitanis mutant pol 6 |
title_auth |
Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 |
abstract |
Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $. © Humana Press Inc 2005 |
abstractGer |
Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $. © Humana Press Inc 2005 |
abstract_unstemmed |
Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $. © Humana Press Inc 2005 |
collection_details |
GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_40 GBV_ILN_65 GBV_ILN_70 GBV_ILN_105 GBV_ILN_4012 GBV_ILN_4219 GBV_ILN_4310 |
container_issue |
2 |
title_short |
Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6 |
url |
https://doi.org/10.1385/ABAB:125:2:099 |
remote_bool |
false |
author2 |
Mechichi, Tahar Limam, Ferid Marzouki, Nejib |
author2Str |
Mechichi, Tahar Limam, Ferid Marzouki, Nejib |
ppnlink |
182278573 |
mediatype_str_mv |
n |
isOA_txt |
false |
hochschulschrift_bool |
false |
doi_str |
10.1385/ABAB:125:2:099 |
up_date |
2024-07-04T05:27:04.467Z |
_version_ |
1803624984824774656 |
fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">OLC2130512496</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506021542.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">230506s2005 xx ||||| 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1385/ABAB:125:2:099</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC2130512496</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-He213)ABAB:125:2:099-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="a">540</subfield><subfield code="a">660</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">42.00</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Chaabouni, Semia Ellouz</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Purification and characterization of two low molecular weight endoglucanases produced by Penicillium occitanis mutant pol 6</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2005</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">© Humana Press Inc 2005</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Two endoglucanases (EGs), EG A and EG B, were purified to homogeneity from Penicillium occitanis mutant Pol6 culture medium. The molecular weights of EGA and EGB were 31,000 and 28,000 kDa, respectively. The pI was about 3 for EG A and 7.5 for EG B. Optimal activity was obtained at pH 3.5 for both endoglucanases. Optimal temperature for enzyme activity was 60°C for EG A and 50°C for EG B. EG A was thermostable at 60°C and remained active after 1 h at 70°C. EGs hydrolyzed carboxymethylcellulose, phosphoric acid swollen cellulose, and ß-glucan efficiently, whereas microcrystalline cellulose (Avicel) and laminarin were poorly hydrolyzed. Only EG B showed xylanase activity. Furthermore, these EGs were insensitive to the action of glucose and cellobiose but were inhibited by the divalent cations $ Hg^{2+} $, $ Co^{2+} $, and $ Mn^{2+} $.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Mechichi, Tahar</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Limam, Ferid</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Marzouki, Nejib</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Applied biochemistry and biotechnology / A</subfield><subfield code="d">Humana Press, 1994</subfield><subfield code="g">125(2005), 2 vom: Mai, Seite 99-112</subfield><subfield code="w">(DE-627)182278573</subfield><subfield code="w">(DE-600)1193054-8</subfield><subfield code="w">(DE-576)043085105</subfield><subfield code="x">0273-2289</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:125</subfield><subfield code="g">year:2005</subfield><subfield code="g">number:2</subfield><subfield code="g">month:05</subfield><subfield code="g">pages:99-112</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">https://doi.org/10.1385/ABAB:125:2:099</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">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">GBV_ILN_21</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_65</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_105</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_4219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4310</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">42.00</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">125</subfield><subfield code="j">2005</subfield><subfield code="e">2</subfield><subfield code="c">05</subfield><subfield code="h">99-112</subfield></datafield></record></collection>
|
score |
7.397299 |