kCAT Inactivation of mushroom polyphenol oxidase
β Scribed by Avi Golan-Goldhirsh; John R. Whitaker
- Publisher
- Elsevier Science
- Year
- 1985
- Weight
- 578 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0304-5102
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Polyphenol oxidase in chloroform was shown to have increased catalytic efficiency, and to transform sterically more demanding substrates, in the presence of SDS, compared with its absence. The limited protein flexibility due to chloroform were apparently altered by the SDS, with little loss of activ
## Abstract Polyphenol oxidase (PPO) obtained from wheat bran catalyzed the oxidation of 4βmethyl catechol. Phenolic compounds found naturally in crude extract played role as an endogeneous substrate and activity of crude extract needed correction. Activity versus enzyme concentration gave a linear