Partial purification of polyphenol oxidase from plums (Prunus domestica L., cv. Stanley)
Polyphenol oxidase (PPO) was extracted and purified from Stanley plums (Prunus domestica L.). Crude PPO showed pH optima of 5.8 to 6.4 with different substrates. Heating for 5 min at 75 C completely inactivated this enzyme. Plum PPO was stable at -20 C for 16 weeks. Km of this enzyme ranged from 17....
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Published in | Journal of food biochemistry Vol. 20; no. 5; pp. 111 - 123 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Oxford, UK
Blackwell Publishing Ltd
01.10.1996
Blackwell |
Subjects | |
Online Access | Get full text |
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Summary: | Polyphenol oxidase (PPO) was extracted and purified from Stanley plums (Prunus domestica L.). Crude PPO showed pH optima of 5.8 to 6.4 with different substrates. Heating for 5 min at 75 C completely inactivated this enzyme. Plum PPO was stable at -20 C for 16 weeks. Km of this enzyme ranged from 17.5 mM with 4-methylcatechol to 31.2 mM with chlorogenic acid. The enzyme was purified 36-fold through (NH4)2SO4 fractionation and chromatography on DEAE-cellulose and Sephadex G-100. PAGE of crude and purified plum PPO showed 7 and 3 bands, respectively, when stained for activity with catechol. The molecular weight of 3 subunits of purified PPO was estimated in the range of 45-66kD |
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Bibliography: | Q04 1997066152 istex:3505C20DCCAA06E56329DBEB544C57198BD4EB68 ArticleID:JFBC111 ark:/67375/WNG-BCXVWB99-J |
ISSN: | 0145-8884 1745-4514 |
DOI: | 10.1111/j.1745-4514.1996.tb00576.x |