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dc.contributor.authorXu, JS
dc.contributor.author徐金森
dc.contributor.authorZheng, TL
dc.contributor.author郑天凌
dc.contributor.authorMeguro, S
dc.contributor.authorKawachi, S
dc.date.accessioned2011-10-23T01:40:53Z
dc.date.available2011-10-23T01:40:53Z
dc.date.issued2004
dc.identifier.citationJournal of Wood Science ,Volume 50, Number 3, 260-265zh_CN
dc.identifier.issn1435-0211
dc.identifier.urihttp://dx.doi.org/doi:10.1007/s10086-003-0554-6
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10976
dc.description.abstractPolyphenol oxidase from Castanea henryi nuts was partially purified. Some characteristics of the enzyme were then determined to help devise measures for the prevention of undesirable enzymatic browning during storage and processing of the nuts. Preparation of acetone powder extracts of the nuts, ammonium sulfate precipitation, dialysis, and gel filtration resulted in 37-fold purification of the enzyme with a yield of 13%. Sodium dodecyl sulfate-polyacrylamide get electrophoresis and the excitation spectrum confirmed the enzyme preparation to be homogeneous. The approximate molecular weight of the enzyme was determined by gel filtration to be 69 kD. The enzyme catalyzed the oxidation of catechol and pyrogallic acid as substrates but did not affect cresol or tyrosine. Using catechol as substrate, p-nitrophenol, thiourea, orcinol, and naphthol showed strong inhibition. The optimal pH and temperature for the enzyme were pH 5.0 and 40degreesC, respectively. The enzyme proved heat labile. When the enzyme was incubated at 70degreesC for 30 min, the remaining activity of the enzyme was only 8%. Possible approaches to applying the results of this study to the prevention of enzymatic browning in the production of C. henryi nuts is also discussed.zh_CN
dc.language.isoenzh_CN
dc.publisherSPRINGER TOKYOzh_CN
dc.subjectpolyphenol oxidasezh_CN
dc.subjectenzymatic browningzh_CN
dc.subjectCastanea henryi nutszh_CN
dc.subjectpurificationzh_CN
dc.subjectinhibitionzh_CN
dc.titlePurification and characterization of polyphenol oxidase from Henry chestnuts (Castanea henryi)zh_CN
dc.typeArticlezh_CN


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