Biochemical studies of cocoa bean polyphenol oxidase

Polyphenol oxidase (EC 1.14.18.1) was isolated and partially purified from cocoa beans. The properties of the enzyme were studied. The Michaelis constant Km for catechol was 1 × 10−2 M. The pH optimum of polyphenol oxidase activity assayed with catechol as substrate occurred at pH 6.8 and was charac...

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Main Authors: Pat, M Lee, Kong, Hung Lee, Abdul Karim, Mohd Ismail
Format: Article
Published: John Wiley & Sons 1991
Online Access:http://psasir.upm.edu.my/id/eprint/115537/
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author Pat, M Lee
Kong, Hung Lee
Abdul Karim, Mohd Ismail
author_facet Pat, M Lee
Kong, Hung Lee
Abdul Karim, Mohd Ismail
author_sort Pat, M Lee
building UPM Institutional Repository
collection Online Access
description Polyphenol oxidase (EC 1.14.18.1) was isolated and partially purified from cocoa beans. The properties of the enzyme were studied. The Michaelis constant Km for catechol was 1 × 10−2 M. The pH optimum of polyphenol oxidase activity assayed with catechol as substrate occurred at pH 6.8 and was characterised by a relatively high thermal stability, 50% of its activity was lost after heating for 40, 25 and 5 min at 60, 69 and 80°C respectively. The optimum temperature for the enzyme activity with catechol as substrate was around 45°C. The enzyme was reactive towards 3‐(3,4‐dihydroxy phenyl)‐DL‐alanine, 3‐hydroxytyramine hydrochloride and 4‐methyl catechol but showed no activity towards tyrosine, p‐cresol, and 4‐hydroxy‐phenol. A rapid deactivation of the enzyme was observed when catechol of concentration > 40 mM was used as substrate. The enzyme activity was inhibited by ascorbic acid, L‐cysteine, sodium bisulphite and thiourea.
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spelling upm-1155372025-03-07T00:15:58Z http://psasir.upm.edu.my/id/eprint/115537/ Biochemical studies of cocoa bean polyphenol oxidase Pat, M Lee Kong, Hung Lee Abdul Karim, Mohd Ismail Polyphenol oxidase (EC 1.14.18.1) was isolated and partially purified from cocoa beans. The properties of the enzyme were studied. The Michaelis constant Km for catechol was 1 × 10−2 M. The pH optimum of polyphenol oxidase activity assayed with catechol as substrate occurred at pH 6.8 and was characterised by a relatively high thermal stability, 50% of its activity was lost after heating for 40, 25 and 5 min at 60, 69 and 80°C respectively. The optimum temperature for the enzyme activity with catechol as substrate was around 45°C. The enzyme was reactive towards 3‐(3,4‐dihydroxy phenyl)‐DL‐alanine, 3‐hydroxytyramine hydrochloride and 4‐methyl catechol but showed no activity towards tyrosine, p‐cresol, and 4‐hydroxy‐phenol. A rapid deactivation of the enzyme was observed when catechol of concentration > 40 mM was used as substrate. The enzyme activity was inhibited by ascorbic acid, L‐cysteine, sodium bisulphite and thiourea. John Wiley & Sons 1991 Article PeerReviewed Pat, M Lee and Kong, Hung Lee and Abdul Karim, Mohd Ismail (1991) Biochemical studies of cocoa bean polyphenol oxidase. Journal of the Science of Food and Agriculture, 55 (2). pp. 251-260. ISSN 0022-5142; eISSN: 1097-0010 https://onlinelibrary.wiley.com/doi/10.1002/jsfa.2740550210 10.1002/jsfa.2740550210
spellingShingle Pat, M Lee
Kong, Hung Lee
Abdul Karim, Mohd Ismail
Biochemical studies of cocoa bean polyphenol oxidase
title Biochemical studies of cocoa bean polyphenol oxidase
title_full Biochemical studies of cocoa bean polyphenol oxidase
title_fullStr Biochemical studies of cocoa bean polyphenol oxidase
title_full_unstemmed Biochemical studies of cocoa bean polyphenol oxidase
title_short Biochemical studies of cocoa bean polyphenol oxidase
title_sort biochemical studies of cocoa bean polyphenol oxidase
url http://psasir.upm.edu.my/id/eprint/115537/
http://psasir.upm.edu.my/id/eprint/115537/
http://psasir.upm.edu.my/id/eprint/115537/