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Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64 |
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| Authors: | Dessy Natalia Keni Vidilaseris Pasjan Satrimafitrah Wangsa T. Ismaya Purkan Hjalmar Permentier Guntur Fibriansah Fernita Puspasari Zeily Nurachman Bauke W. Dijkstra Soetijoso Soemitro |
| Affiliation: | 1. Division of Biochemistry, Faculty of Mathematics and Natural Sciences, Bandung Institute of Technology, Jl. Ganesa 10, 40132, Bandung, Indonesia 2. Protein X-ray Crystallography, Laboratory of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands 3. Laboratory of Biochemistry, Department of Chemistry, Padjajaran University, Jl. Singaperbangsa 2, 40133, Bandung, Indonesia 5. Mass Spectrometry Core Facility, University of Groningen, Antonius Deusinglaan 1, 9713 AV, Groningen, The Netherlands |
| 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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