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: Lee, Pat M, Lee, Kong‐Hung, Ismail, Mohd, Karim, Abdul
Format: Article
Published: John Wiley & Sons 1991
Online Access:http://psasir.upm.edu.my/id/eprint/116312/
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author Lee, Pat M
Lee, Kong‐Hung
Ismail, Mohd
Karim, Abdul
author_facet Lee, Pat M
Lee, Kong‐Hung
Ismail, Mohd
Karim, Abdul
author_sort Lee, Pat M
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-1163122025-03-25T01:28:04Z http://psasir.upm.edu.my/id/eprint/116312/ Biochemical studies of cocoa bean polyphenol oxidase Lee, Pat M Lee, Kong‐Hung Ismail, Mohd Karim, Abdul 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 Lee, Pat M and Lee, Kong‐Hung and Ismail, Mohd and Karim, Abdul (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 Lee, Pat M
Lee, Kong‐Hung
Ismail, Mohd
Karim, Abdul
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/116312/
http://psasir.upm.edu.my/id/eprint/116312/
http://psasir.upm.edu.my/id/eprint/116312/