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A thermostable maltose‐tolerant α‐amylase from Aspergillus tamarii
Author(s) -
Moreira Fabiana Guillen,
Lenartovicz Veridiana,
Peralta Rosane Marina
Publication year - 2004
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.200310302
Subject(s) - maltotriose , maltose , amylopectin , amylose , starch , chemistry , amylase , hydrolysis , enzyme , alpha amylase , polysaccharide , substrate (aquarium) , homogeneous , biochemistry , chromatography , food science , biology , ecology , physics , thermodynamics
Abstract An homogeneous fraction of α‐amylase from Aspergillus tamarii was obtained by means of a very easy purification procedure. The enzyme is a glycoprotein containing 32% saccharide and MW of 37.5 kDa. Optimal of pH and temperature with starch as substrate were 4.5–6.5 and 50–55 °C. The enzyme was stable for several hours at temperature up to 65 °C. Starch, amylose, and amylopectin were the substrates preferentially hydrolysed and maltose and maltotriose were the main end products. The values of K M and V max for starch were 2 g/l and 880 μmoles reducing sugars/min.mg of protein, respectively. The purified enzyme was remarkably insensitive to end product inhibition, being only slightly inhibited by maltose and glucose up to 1.0 M .