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Isolation and Some Properties of Amylase from Streptomyces hygroscopicus SF‐1084
Author(s) -
Hidaka H.,
Koaze Y.,
Yoshida K.,
Niwa T.,
Shomura T.,
Niida T.
Publication year - 1974
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19740261204
Subject(s) - amylase , maltose , starch , chemistry , amylopectin , sephadex , chromatography , streptomyces hygroscopicus , amylose , food science , hydrolysis , ammonium sulfate precipitation , biochemistry , sucrose , streptomyces , enzyme , biology , bacteria , size exclusion chromatography , genetics
After screening about three thousands of Streptomyces strains from soils, a strain of Streptomyces hygroscopicus SF‐1084, which gave the highest amylase production was isolated and some properties of the amylase were studied. Amylase production media were examined and a medium which consisted of glucose 2%, corn starch 5.5%, corn meal 1%, wheat germ 0.5%, soy bean meal 1.4%, KH 2 PO 4 0.2% adjusted to pH 7.0 was used to produce the amylase. Amylase production by 30 l jar fermenter was reached at 1500 u/ml in 110 h culture. The amylase was purified from broth filtrate by the method of ammonium sulfate precipitation, DEAE‐sephadex A‐50 column chromatography and Sephadex G‐150 gelfiltration to get single band on a polyacrylamide disc gel electrophoresis. It is shown that the SF‐1084 amylase produced 88% maltose from amylose and 80% maltose from amylopectin in 48 h saccharification. From the pattern of blue value and reducing value, the amylase is supposed to have endogenous action on starch and the activity is not inhibited by PCNB (pentachloronitrobenzene); the SF‐1084 amylase does not belong to β‐amylase. The optimum pH of the amylase was 5 to 6 and the optimum temperature was 50 to 55 °C. The amylase was fairly thermostable and the residual activity after incubation at 90 °C for 15 min and 100 °C for 15 min were revealed more than 50% and 30% respectively.