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PURIFICATION AND PARTIAL CHARACTERIZATION OF TYROSINASE ISOFORMS FROM CAP FLESH OF PORTABELLA MUSHROOMS
Author(s) -
ZHANG XIAODONG,
FLURKEY WILLIAM H.
Publication year - 1999
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1999.tb00007.x
Subject(s) - tyrosinase , chemistry , enzyme , flesh , gene isoform , chromatography , yield (engineering) , biochemistry , molecular mass , protein subunit , ion chromatography , food science , gene , materials science , metallurgy
Tyrosinase was isolated from the cap flesh of Portabella mushrooms. Several mg of enzyme were isolated with an overall yield of 18%. Large DEAE ion exchange columns and selective pooling of fractions, followed by chromatography of pooled fractions on hydroxylapatite columns resulted in the isolation of highly purified tyrosinase. The isolated enzymes had apparent subunit molecular weights of approximately 48–50 kDa and pIs from 5.1 to 5.3. The purification scheme can be carried out rapidly and has the potential to separate different groups of tyrosinase isoforms.