Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

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 activi...

Full description

Saved in:
Bibliographic Details
Published in:Biológia 2011-02, Vol.66 (1), p.27-32
Main Authors: Natalia, Dessy, Vidilaseris, Keni, Satrimafitrah, Pasjan, Ismaya, Wangsa T., Purkan, Permentier, Hjalmar, Fibriansah, Guntur, Puspasari, Fernita, Nurachman, Zeily, Dijkstra, Bauke W., Soemitro, Soetijoso
Format: Article
Language:English
Subjects:
Biomedical and Life Sciences
Cell Biology
glucoamylase
Life Sciences
Microbiology
Plant Sciences
raw starch binding
Saccharomycopsis fibuligera R64
Section Cellular and Molecular Biology
thermostable
variation between strains
Zoology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 IC 50 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.
ISSN:0006-3088
1336-9563
DOI:10.2478/s11756-010-0151-2