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- W2092716859 abstract "The amylases produced by a Bacillus stearothermophilus were purified through a series of four steps. Two separable enzyme fractions having starch hydrolysing activity were eluted from a DEAE-cellulose column by NaCl gradient elution. The homogeneity of the purified enzymes was checked on polyacrylamide gel electrophoresis. The product formation studies indicated that fraction I was an α-amylase whereas fraction II was a β-amylase. The molecular weights were determined to be 48 000 and 57 000 and the carbohydrate moiety was found to be 13.2 and 0.8% for α- and β-amylase, respectively. The protein digest of these enzymes indicated a total number of 15 amino acids with aspartic and glutamic acid showing the highest value. The purified amylase showed maximal activity at 80°C and pH 6.9. Fe3+, Cd2+, Pb2+, Hg2+, Ni2+ and Ag1+ were potent inhibitors whereas Zn2+, Mg2+, Mn2+ and Al3+ were mild inhibitors. Ca2+, Ba2+, Sr2+ and K+ stimulated amylase activity in the order of Ca2+ > Ba2+ > Sr2+ > K+. PCMB, EDTA and sodium iodoacetate were inhibitory whereas glutathione (GSH) and cysteine afforded protection of enzyme activity. EDTA showed dose-dependent noncompetitive inhibition of both α- as well as β-amylase activities. EDTA inhibition was reversed by the addition of Ca2+ and PCMB inhibition by the addition of glutathione (reduced). The Km for α- and β-amylases were found to be 1.05 and 1.25 mg starch per ml, respectively." @default.
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- W2092716859 date "1987-12-01" @default.
- W2092716859 modified "2023-09-24" @default.
- W2092716859 title "Purification and chemical characterization of thermostable amylases produced by Bacillus stearothermophilus" @default.
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- W2092716859 doi "https://doi.org/10.1016/0141-0229(87)90036-6" @default.
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