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Cloning and some properties of Japanese pear ( Pyrus pyrifolia ) polyphenol oxidase, and changes in browning potential during fruit maturation
Author(s) -
Nishimura Makiyo,
Fukuda Chieko,
Murata Masatsune,
Homma Seiichi
Publication year - 2003
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.1518
Subject(s) - polyphenol oxidase , browning , pear , biochemistry , polyphenol , biology , plastid , oxidase test , chemistry , botany , enzyme , gene , antioxidant , peroxidase , chloroplast
A PCR‐amplified genomic DNA fragment encoding Japanese pear ( Pyrus pyrifolia ) polyphenol oxidase (PPO) was cloned and sequenced. The DNA appears to encode a 66 kDa precursor protein consisting of a 56 kDa mature protein and a 9.5 kDa N‐terminal transit peptide. The amino acid sequence showed high homology with apple PPO. The PPO mainly existed as a soluble fraction in cells and was limitedly proteolysed, while the mature form (56 kDa) was detected in plastids. Immature fruits showing high browning potential had high PPO activity and a high level of phenolics, while mature fruits showing little browning had high PPO activity but a low level of phenolics. Copyright © 2003 Society of Chemical Industry