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Purification of Polyphenoloxidase from the Purple‐fleshed Potato ( Solanum tuberosum Jasim) and its Secondary Structure
Author(s) -
Jang J.,
Song K.B.
Publication year - 2004
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2004.tb18012.x
Subject(s) - solanum tuberosum , chemistry , gel permeation chromatography , chromatography , polyacrylamide gel electrophoresis , polyphenol oxidase , molecular mass , gel electrophoresis , sodium dodecyl sulfate , enzyme , size exclusion chromatography , ammonium sulfate , circular dichroism , biochemistry , botany , biology , peroxidase , organic chemistry , polymer
Polyphenoloxidase (PPO) was purified from purple‐fleshed potatoes ( Solanum tuberosum Jasim) using membrane concentration, ammonium sulfate fractionation, Resource Q ion exchange chromatography, and Sephacryl S‐200 HR gel permeation chromatography. PPO was purified 78‐fold from a crude extract. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis results showed that the purified enzyme has a major subunit molecular weight of 40 kDa. To elucidate the secondary structure of the purified PPO, circular dichroism (CD) was performed. The CD spectrum of the purified enzyme showed that PPO contains 35% α‐helix, 30% β‐turn, and 35% random coil structure.