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- W2092129614 abstract "Abstract β-Amylase was purified from tap roots of alfalfa (cv Hi-Phy) using techniques to enrich β-amylase activity, while simultaneously separating it from α-amylase activity. Proteins in crude extracts were precipitated with polyethylene glycol and ethanol, followed by ammonium sulphate fractionation, gel filtration and ion exchange chromatography. The purified β-amylase migrated as a single polypeptide with a M r of 57 500 using SDS-PAGE. When electrophoresed using native polyacrylamide gel electrophesis and blotted into starch-containing gels, several β-amylase isoforms were evident. β-Amylase from alfalfa tap roots readily hydrolysed amylopectin, and to a lesser extent, soluble starch, releasing maltose. It also hydrolysed amylose and glycogen; however, activity was lower with these glucans than with amylopectin or soluble starch. No activity was detected when β-limit dextrin was used as substrate. The purified β-amylase had a pH optimum of 7.5, which is higher than those from most other sources." @default.
- W2092129614 created "2016-06-24" @default.
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- W2092129614 date "1992-02-01" @default.
- W2092129614 modified "2023-09-25" @default.
- W2092129614 title "β-amylase from tap roots of alfalfa" @default.
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- W2092129614 doi "https://doi.org/10.1016/0031-9422(92)90011-e" @default.
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