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TENDERIZATION OF MEAT WITH PAPAYA LATEX PROTEASES
Author(s) -
KANG C. K.,
WARNER W. D.
Publication year - 1974
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.1365-2621.1974.tb17985.x
Subject(s) - papain , chymopapain , proteases , protease , thermostability , chemistry , carica , food science , enzyme , biochemistry , denaturation (fissile materials) , biology , botany , nuclear chemistry
ABSTRACTS Tenderization of meat by papaya latex preparations was achieved by the combined action of several proteases. Both in vitro and in vivo application of enzymes gave degradation of muscle proteins, and degradation of connective tissue only after heat denaturation. Purified papaya enzymes‐papain, chymopapain and papaya peptidase A‐were uniformly distributed throughout the various muscles and in the extravascular system after antemortem injection into the vascular system. Chymopapain was the primary contributor for tenderization because it constituted the major protease in the mixture and it had higher thermostability and more favorable action at the meat's natural pH than papain or papaya peptidase A.