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Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64
Natalia D.a, Vidilaseris K.a, Satrimafitrah P.a, Ismaya W.T.c, Purkana, Permentier H.e, Fibriansah G., Puspasari F.a, Nurachman Z.a, Dijkstra B.W., Soemitro S.c
a Division of Biochemistry, Faculty of Mathematics and Natural Sciences, Bandung Institute of Technology, Indonesia
b Protein X-ray Crystallography, Laboratory of Biochemistry, University of Groningen, Netherlands
c Laboratory of Biochemistry, Department of Chemistry, Padjajaran University, Indonesia
d Department of Biochemistry and Cell Biology, Veterinary Medicine, University of Utrecht, Netherlands
e Mass Spectrometry Core Facility, University of Groningen, Netherlands
[vc_row][vc_column][vc_row_inner][vc_column_inner][vc_separator css=”.vc_custom_1624529070653{padding-top: 30px !important;padding-bottom: 30px !important;}”][/vc_column_inner][/vc_row_inner][vc_row_inner layout=”boxed”][vc_column_inner width=”3/4″ css=”.vc_custom_1624695412187{border-right-width: 1px !important;border-right-color: #dddddd !important;border-right-style: solid !important;border-radius: 1px !important;}”][vc_empty_space][megatron_heading title=”Abstract” size=”size-sm” text_align=”text-left”][vc_column_text]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. © 2011 Versita Warsaw and Springer-Verlag Wien.[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Author keywords” size=”size-sm” text_align=”text-left”][vc_column_text][/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Indexed keywords” size=”size-sm” text_align=”text-left”][vc_column_text]Glucoamylase,Raw starch binding,Saccharomycopsis fibuligera R64,Thermostable,Variation between strains[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Funding details” size=”size-sm” text_align=”text-left”][vc_column_text]The research was supported by the Ministry of National Education, Indonesia (for KV via Beasiswa Unggulan) and Bandung Institute of Technology (for DN via Riset Ung-gulan project, contract number: 0021/K01.03.2/PL2.15/I/ 2008).[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”DOI” size=”size-sm” text_align=”text-left”][vc_column_text]https://doi.org/10.2478/s11756-010-0151-2[/vc_column_text][/vc_column_inner][vc_column_inner width=”1/4″][vc_column_text]Widget Plumx[/vc_column_text][/vc_column_inner][/vc_row_inner][/vc_column][/vc_row][vc_row][vc_column][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][/vc_column][/vc_row]