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Purification and Characterization of Alkaline Proteinase from Atlantic Menhaden Muscle
Author(s) -
Choi Y.J.,
Lanier T.C.,
Lee H.G.,
Cho Y.J.
Publication year - 1999
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.1365-2621.1999.tb15908.x
Subject(s) - alkaline protease , chemistry , homogeneous , enzyme , chromatography , biochemistry , thermal stability , serine , organic chemistry , protease , physics , thermodynamics
Two alkaline proteinases (A and B) were isolated and found to be composed of homogeneous subunits. These proteinases, A and B, were concentrated 62.9‐and 986.5‐fold compared to the crude muscle extract, with molecular weights of 707,000 and 450,000, respectively. Both are probably serine type proteinases, and optimum caseinolytic activity was shown at pH 8.0 and 55 °C. Both degraded actomyosin under similar conditions. Enzyme A had higher thermal stability than B. The residual activities of A and B in 3.6% NaCl solution were 95% and 85%. These data suggest that these proteinases are involved in the softening of menhaden surimi gels which occurs during heating at 50 to 70 °C.