Article ID Journal Published Year Pages File Type
10233238 Enzyme and Microbial Technology 2005 5 Pages PDF
Abstract
An α-amylase was purified from marine Vibrio sp. using starch affinity method with molecular mass of 52.480 kDa. This amylase showed maximum activity at 55-60 °C and pH 6.5 and retain 85% of maximal activity after 30 min preincubation at 65 °C. The enzyme was inhibited by ethylenediaminetetra-acetate (EDTA) and [ethylenebis(oxonitrilo)]tetra-acetate (EGTA) while divalent metal ions, such as Fe2+, Mn2+, Co2+, Ca2+, Mg2 and Cu2+ could restored near 25-55% of maximal activity suggesting that the metal ions need for the enzyme activity. Digestion of corn-starch by the enzyme showed random cleavage with various sizes of products, indicating endo action of the enzyme. Chemical modification suggested involvement of Lys, Trp, Asp/Glu and His in the enzyme activity. The starch affinity method used here showed high yield purified amylase with very low experimental cost.
Related Topics
Physical Sciences and Engineering Chemical Engineering Bioengineering
Authors
, ,