Alpha-Amylase from Persimmon Honey: Purification and Characterization |
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| Authors: | Takeshi Nagai Reiji Inoue Nobutaka Suzuki Toshio Nagashima |
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| Affiliation: | 1. Department of Food Science and Technology , Tokyo University of Agriculture , Hokkaido, Japan t1nagai@bioindustry.nodai.ac.jp nagatakenagetake@yahoo.co.jp;3. Inoue Yohojo Bee Farm Inc. , Hyogo, Japan;4. Nagoya Research Institute , Toyoake, Aichi, Japan;5. Department of Food Science and Technology , Tokyo University of Agriculture , Hokkaido, Japan |
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| Abstract: | The α-amylase was extracted from pure persimmon honey and purified by DEAE-Toyopearl 650M, CM-Toyopearl 650M, and Toyopearl HW-55F column chromatographies. Molecular weight of purified enzyme was estimated to be about 58 kDa by Toyopearl HW-55F gel chromatography and SDS-PAGE, respectively suggested that the purified enzyme was a monomer. Optimum pH of the enzyme was 6.0?7.0 and optimum temperature 40°C. The enzyme was extremely inactivated at pH was higher than 7.0 or lower than 5.0. Heat inactivation occurred at 40°C. This enzyme activated by Ca 2+ , Mn2+, PCMB, and DTNB, but inhibited by Ba2+, Fe3+, Hg2+, Mg2+, and iodoacetic acid. The purified enzyme was of α?-type by TLC analysis. The relative rate of hydrolysis of the polymeric substance decreased with decreasing percentage of α?-1,4-linkages and with increasing percentage of α?-1,6-linkages in substrate similar to the results from commercially available honey. |
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| Keywords: | Persimmon honey α-amylase Characterization |
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