Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

Dessy Natalia, Keni Vidilaseris, Pasjan Satrimafitrah, Wangsa T. Ismaya, Purkan, Hjalmar Permentier, Guntur Fibriansah, Fernita Puspasari, Zeily Nurachman, Bauke W. Dijkstra, Soetijoso Soemitro

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)27-32
Number of pages6
JournalBiologia (Poland)
Issue number1
Publication statusPublished - 2011
Externally publishedYes


  • Glucoamylase
  • Raw starch binding
  • Saccharomycopsis fibuligera R64
  • Thermostable
  • Variation between strains


Dive into the research topics of 'Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64'. Together they form a unique fingerprint.

Cite this