Premium
HYDROPHOBIC ADSORPTION CHROMATOGRAPHY OF PEACH POLYPHENOL OXIDASE
Author(s) -
FLURKEY WILLIAM H.,
JEN JOSEPH J.
Publication year - 1980
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.1365-2621.1980.tb07576.x
Subject(s) - chemistry , sepharose , polyphenol oxidase , agarose , alkyl , adsorption , chromatography , hydrophilic interaction chromatography , phenylalanine , affinity chromatography , phenol , hydrophobic effect , phenols , enzyme , organic chemistry , amino acid , biochemistry , high performance liquid chromatography , peroxidase
Peach fruit polyphenol oxidase, both crude and pure preparations, were found to adsorb to Phenyl Sepharose, 4‐phenylbutylamine Sepharose, CBZ‐phenylalanine‐TETA‐alkyl Sepharose, octyl‐ and decyl‐agarose columns. The enzyme showed no affinity to amino‐alkyl agaroses, hydrophobic media with terminal phenol, amino, or carboxyl groups on the ligands. The enzyme is weakly hydrophobic and can be purified and characterized with hydrophobic chromatography. Phenyl Sepharose CL‐4B columns gave the best separation of isoenzyme forms of the enzyme probably due to biospecitic effect in addition to the hydrophobic interactions.