Publication: Polyphenol oxidases from latex of Hevea brasiliensis: Purification and characterization
Issued Date
2002-09-13
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ISSN
00319422
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2-s2.0-0037072724
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Mahidol University
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SCOPUS
Bibliographic Citation
Phytochemistry. Vol.61, No.2 (2002), 115-121
Suggested Citation
Dhirayos Wititsuwannakul, Nopphakaew Chareonthiphakorn, Mario Pace, Rapepun Wititsuwannakul Polyphenol oxidases from latex of Hevea brasiliensis: Purification and characterization. Phytochemistry. Vol.61, No.2 (2002), 115-121. doi:10.1016/S0031-9422(02)00234-0 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/19970
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Title
Polyphenol oxidases from latex of Hevea brasiliensis: Purification and characterization
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Abstract
Polyphenol oxidase (PPO) was isolated from the B-serum obtained after repetitive freeze-thawing of the bottom fraction isolated from ultracentrifuged fresh latex. The B-serum was subjected to acetone precipitation and CM-Sepharose chromatography, affording two PPOs, PPO-I and PPO-II, which, upon SDS-PAGE, were 32 and 34 kDa, respectively. Both PPOs possessed the same pI (9.2), optimum pH (7) and optimum temperature (35-45 °C). They are stable up to 60 °C and active at broad pH ranges from 4-9. The Kmvalues of PPO-I for dopamine, L-dopa and catechol as substrates are 2.08, 8.33 and 9.09 mM, while those for PPO-II are 2.12, 4.76 and 7.14 mM, respectively. Among various PPO inhibitors tested, 4-hexylresorcinol was the most potent. Anionic detergents were among the most effective activators of the enzymes, while cationic and nonionic detergents showed little and no effect on the PPO activities, respectively. © 2002 Elsevier Science Ltd. All rights reserved.