A novel thermostable α-galactosidase from the thermophilic fungus Thermomyces lanuginosus CBS 395.62/b: Purification and characterization
High levels of an extracellular α-galactosidase are produced by the thermophilic fungus Thermomyces lanuginosus CBS 395.62/b when grown in submerse culture and induced by sucrose. The enzyme was purified 114-fold from the culture supernatant by (NH 4) 2SO 4 fractionation, and by chromatographical st...
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| Published in | Biochimica et biophysica acta. General subjects Vol. 1770; no. 1; pp. 55 - 62 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Elsevier B.V
2007
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| Subjects | |
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| Abstract | High levels of an extracellular α-galactosidase are produced by the thermophilic fungus
Thermomyces lanuginosus CBS 395.62/b when grown in submerse culture and induced by sucrose. The enzyme was purified 114-fold from the culture supernatant by (NH
4)
2SO
4 fractionation, and by chromatographical steps including Sepharose CL-6B gel filtration, DEAE-Sepharose FF anion-exchange, Q-Sepharose FF anion-exchange and Superose 12 gel filtration. The purified enzyme exhibits apparent homogeneity as judged by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and iso-electric focusing (IEF). The native molecular weight of the monomeric α-galactosidase is 93 kDa with an isoelectric point of 3.9. The enzyme displays a pH and temperature optimum of 5–5.5 and 65 °C, respectively. The purified enzyme retains more than 90% of its activity at 45 °C in a pH range from 5.5 to 9.0. The enzyme proves to be a glycoprotein and its carbohydrate content is 5.3%. Kinetic parameters were determined for the substrates
p-nitrophenyl-α-galactopyranoside, raffinose and stachyose and very similar
K
m values of 1.13 mM, 1.61 mM and 1.17 mM were found. Mn
++ ions activates enzyme activity, whereas inhibitory effects can be observed with Ca
++, Zn
++ and Hg
++. Five min incubation at 65° with 10 mM Ag
+ results in complete inactivation of the purified α-galactosidase. Amino acid sequence alignment of
N-terminal sequence data allows the α-galactosidase from
Thermomyces lanuginosus to be classified in glycosyl hydrolase family 36. |
|---|---|
| AbstractList | High levels of an extracellular α-galactosidase are produced by the thermophilic fungus
Thermomyces lanuginosus CBS 395.62/b when grown in submerse culture and induced by sucrose. The enzyme was purified 114-fold from the culture supernatant by (NH
4)
2SO
4 fractionation, and by chromatographical steps including Sepharose CL-6B gel filtration, DEAE-Sepharose FF anion-exchange, Q-Sepharose FF anion-exchange and Superose 12 gel filtration. The purified enzyme exhibits apparent homogeneity as judged by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and iso-electric focusing (IEF). The native molecular weight of the monomeric α-galactosidase is 93 kDa with an isoelectric point of 3.9. The enzyme displays a pH and temperature optimum of 5–5.5 and 65 °C, respectively. The purified enzyme retains more than 90% of its activity at 45 °C in a pH range from 5.5 to 9.0. The enzyme proves to be a glycoprotein and its carbohydrate content is 5.3%. Kinetic parameters were determined for the substrates
p-nitrophenyl-α-galactopyranoside, raffinose and stachyose and very similar
K
m values of 1.13 mM, 1.61 mM and 1.17 mM were found. Mn
++ ions activates enzyme activity, whereas inhibitory effects can be observed with Ca
++, Zn
++ and Hg
++. Five min incubation at 65° with 10 mM Ag
+ results in complete inactivation of the purified α-galactosidase. Amino acid sequence alignment of
N-terminal sequence data allows the α-galactosidase from
Thermomyces lanuginosus to be classified in glycosyl hydrolase family 36. |
| Author | Braet, Christophe Hoschke, Ágoston Claeyssens, Marc Hajós, Gyöngyi Nguyen, Quang D. Rezessy-Szabó, Judit M. |
| Author_xml | – sequence: 1 givenname: Judit M. surname: Rezessy-Szabó fullname: Rezessy-Szabó, Judit M. email: judit.szabo@uni-corvinus.hu organization: Department of Brewing and Distilling, Faculty of Food Science, Corvinus University of Budapest, H-1118 Budapest, Ménesi út 45, Hungary – sequence: 2 givenname: Quang D. surname: Nguyen fullname: Nguyen, Quang D. organization: Department of Brewing and Distilling, Faculty of Food Science, Corvinus University of Budapest, H-1118 Budapest, Ménesi út 45, Hungary – sequence: 3 givenname: Ágoston surname: Hoschke fullname: Hoschke, Ágoston organization: Department of Brewing and Distilling, Faculty of Food Science, Corvinus University of Budapest, H-1118 Budapest, Ménesi út 45, Hungary – sequence: 4 givenname: Christophe surname: Braet fullname: Braet, Christophe organization: Laboratory of Glycobiology, Department of Biochemistry, Physiology and Microbiology, Ghent University, B 9000, K.L. Ledeganckstraat, Gent, Belgium – sequence: 5 givenname: Gyöngyi surname: Hajós fullname: Hajós, Gyöngyi organization: Department of Biochemistry, Central Food Research Institute, H-1022 Budapest, Herman Ottó út 15, Hungary – sequence: 6 givenname: Marc surname: Claeyssens fullname: Claeyssens, Marc organization: Laboratory of Glycobiology, Department of Biochemistry, Physiology and Microbiology, Ghent University, B 9000, K.L. Ledeganckstraat, Gent, Belgium |
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| Keywords | Purification α-Galactosidase Thermophilic fungus Thermomyces lanuginosus |
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