Characterization of α-amylase from mandarin orange honey
作者： Takeshi Nagai , Reiji Inoue , Nobutaka Suzuki , Yasuhiro Tanoue , Norihisa Kai
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摘要: Summaryα-Amylase was purified from mandarin orange honey by DEAE-Toyopearl 650M, CM-Toyopearl and Toyopearl HW-55F column chromatographies, characterized. The molecular weight of the enzyme estimated to be about 58 kDa gel chromatography SDS-PAGE, suggesting that a monomer. exhibited optimum activity at pH 5.0 50°C. Inactivation occurred when lower than 3.0 or higher 9.0. activated Co2+, Mn2+, but inhibited Hg2+, Mg2+, Fe3+. By TLC analysis, this α-type split interior α-1,4-glycosidic bonds in random manner. relative rate hydrolysis polymeric substrate decreased with decreasing percentage α-1,4-linkages increasing α-1,6-linkages similar results commercially available honey.
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