Purification and characterization of two soluble acid invertase isozymes from Japanese pear fruit |
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Authors: | Hashizume Hiroshi Tanase Koji Shiratake Katsuhiro Mori Hitoshi Yamaki Shohei |
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Affiliation: | Laboratory of Horticultural Science, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan. |
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Abstract: | Two isozymes (AIV I and AIV II) of soluble acid invertase (EC 3.2.1.26) were purified from Japanese pear fruit through procedures including (NH(4))(2)SO(4) precipitating, DEAE-Sephacel column chromatography, Concanavalin A (ConA)-Sepharose affinity chromatography, hydroxyapatite column chromatography and Mono Q HR 5/5 column chromatography. The specific activities of purified AIV I and AIV II were 2670 and 2340 (nkat/mg protein), respectively. AIV I was a monomeric enzyme of 80 kDa, while AIV II may be also a monomeric enzyme, which is easy to be cleaved to 52 kDa and 34 kDa polypeptide during preparation by SDS-PAGE. The Km values for sucrose of AIV I and AIV II were 3.33 and 4.58 mM, respectively, and optimum pH of both enzyme activities was pH 4.5. |
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Keywords: | Japanese pear (Pyrus serotina) fruit Soluble acid invertase (AIV EC 3.2.1.26) Enzyme purification Isozymes of AIV |
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