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Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

Abstract

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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Abbreviations

Aspni :

Aspergillus niger

GLA1:

glucoamylase from Saccharomycopsis fibuligera KZ

GLL1:

glucoamylase from Saccharomycopsis fibuligera R64

GLM1:

glucoamylase from Saccharomycopsis fibuligera IFO0111

GLU1:

glucoamylase from Saccharomycopsis fibuligera HUT7212

MES:

2-(N-morpholino)ethanesulfonic acid

MMT:

L-malic-acid-MES-Tris-HCl

Sacfi :

Saccharomycopsis fibuligera

SDS-PAGE:

sodium dodecyl-sulphate polyacrylamide gel electrophoresis

TLC:

thin-layer chromatography

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Correspondence to Dessy Natalia.

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Natalia, D., Vidilaseris, K., Satrimafitrah, P. et al. Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64. Biologia 66, 27–32 (2011). https://doi.org/10.2478/s11756-010-0151-2

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  • DOI: https://doi.org/10.2478/s11756-010-0151-2

Key words

  • glucoamylase
  • Saccharomycopsis fibuligera R64
  • variation between strains
  • thermostable
  • raw starch binding