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PURIFICATION AND CHARACTERIZATION OF A NEUTRAL PROTEASE THAT CONTRIBUTES TO THE UNIQUE FLAVOR AND TEXTURE OF TOFU‐MISOZUKE
Author(s) -
FUNAKI JUNKO,
YANO MIDORI,
MISAKA TAKUMI,
ABE KEIKO,
ARAI SOICHI
Publication year - 1997
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.1745-4514.1997.tb00214.x
Subject(s) - aspergillus oryzae , protease , proteases , flavor , food science , taste , chemistry , enzyme , neutral protease , proteolysis , organoleptic , fermentation , biochemistry , autolysis (biology)
Tofu‐misozuke, a food inherent to the Fukuoka district of Japan is a type of soybean curd fermented in miso (soybean paste), possessing a unique taste and texture. A cheese‐like taste and softness also develops in Tofu‐misozuke during ripening. The changes in Tofu‐misozuke are caused by proteases originating from Koji, one of the raw materials of miso. We examined which of the proteases is the cause of taste and textural‐alterations. The protease was purified by DE52, Sephacryl S‐300, Mono Q, and Superose 12 chromatography. The amino terminal sequence of the purified enzyme is TEVTDXKGDA, in agreement with the sequence of neutral protease II from Aspergillus oryzae. The purified enzyme is a heat stable metallo‐protease. These results indicate that the purified enzyme is highly similar to the neutral protease II of Aspergillus oryzae.