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- W2067046219 abstract "Abstract Spinach polyphenol oxidase was partially purified by using phase partitioning in a solution of Triton X-114 in a latent form, free of phenolics and chlorophylls, with a high recovery rate. The enzyme had both catecholase and cresolase activity. The latter, never before described, presented a lag period which was affected by enzyme and substrate concentration. The K m for p -cresol was 2 mM. Substrate inhibition was seen for catecholase activity when 4-methylcatechol was used. The values found for V max , K m and K si were 244 μM/min, 4.2 mM and 104 mM, respectively. The latent enzyme was activated by trypsin (4.5-fold), by SDS and 1-decanesulphonic acid at detergent concentration of 1 mM, but it was strongly inhibited by CTAB, frost, and SDS at a detergent concentration of 10 mM. Non-ionic detergents did not alter significantly the activity of latent enzyme." @default.
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- W2067046219 date "1989-01-01" @default.
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- W2067046219 title "Triton ×-114 as a tool for purifying spinach polyphenol oxidase" @default.
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- W2067046219 doi "https://doi.org/10.1016/s0031-9422(00)97738-0" @default.
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