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Panasonic DV Studio Software download Dv Studio Software download Update Dv Studio Software updatePurification and characterization of wheat beta-amylase active against exocellular alpha-amylase.
An exocellular alpha-amylase from wheat kernel inhibited by amylolytic enzymes was purified to electrophoretically homogeneous, on polyacrylamide gel electrophoresis, a protein fraction with an estimated molecular weight of 84,000. The purified amylase was stimulated by Mn2+, Mg2+ and spermidine and inhibited by Tris and urea. A beta-amylase was purified to electrophoretically homogeneous and relatively stable fractions from delphinidin-supplemented kernel starch incubated in a buffered pH-5.2 solution for 24 h at 37 degrees C. The purified beta-amylase was activated by Mn2+, Mg2+ and spermidine and inhibited by EDTA, EGTA, urea, citrate and tartrate. Of the ionophores tested, only [I]- and [C1]- in a 1 mM concentration effectively activated the beta-amylase. Enzymic activity of beta-amylase was not affected by Ca2+, Fe3+, Fe2+, Co2+, Zn2+, Pb2+, Cu2+, K+, Na+, NH4+, Cd2+ and Ni2+. Kinetic parameters of purified beta-amylase were determined. The main substrate of this enzyme was starch and the best Km (1.38 g/l) and Ki values (0.8 M) were observed with potato tuber starch. The beta-amylase showed higher affinity for non-reducing ends of oligosaccharides than for the reducing ends. Reaction of stromal endo-beta-amylase with exo-amylase resulted in an enzyme with a high affinity for both soluble and insoluble polymers of amylose.「人生一度」
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