Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

被引：0
|
作者：
Dessy Natalia
Keni Vidilaseris
Pasjan Satrimafitrah
Wangsa T. Ismaya
Hjalmar Purkan
Guntur Permentier
Fernita Fibriansah
Zeily Puspasari
Bauke W. Nurachman
Soetijoso Dijkstra
机构：
[1] Bandung Institute of Technology,Division of Biochemistry, Faculty of Mathematics and Natural Sciences
[2] University of Groningen,Protein X
[3] Padjajaran University,ray Crystallography, Laboratory of Biochemistry
[4] University of Utrecht,Laboratory of Biochemistry, Department of Chemistry
[5] University of Groningen,Department of Biochemistry and Cell Biology, Veterinary Medicine
来源：
Biologia | 2011年 / 66卷
关键词：
glucoamylase; R64; variation between strains; thermostable; raw starch binding;
D O I：
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学科分类号：
摘要：
Glucoamylase from the yeast Saccharomycopsis fibuligera R64 (GLL1) has successfully been purified and characterized. The molecular mass of the enzyme was 56,583 Da as determined by mass spectrometry. The purified enzyme demonstrated optimum activity in the pH range of 5.6–6.4 and at 50°C. The activity of the enzyme was inhibited by acarbose with the IC50 value of 5 μM. GLL1 shares high amino acid sequence identity with GLU1 and GLA1, which are Saccharomycopsis fibuligera glucoamylases from the strains HUT7212 and KZ, respectively. The properties of GLL1, however, resemble that of GLU1. The elucidation of the primary structure of GLL1 contributes to the explanation of this finding.
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页码：27 / 32
页数：5
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