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An Immunological Assessment of Myosin Degradation in Pressurized Chicken Muscle
Author(s) -
Kamiyama K.,
Ikeuchi Y.,
Suzuki A.,
Kim K.,
Hayashi T.,
Ito T.
Publication year - 2001
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.1365-2621.2001.tb16092.x
Subject(s) - myosin , cathepsin , cathepsin b , chemistry , cathepsin d , high pressure , cathepsin l , biochemistry , enzyme , microbiology and biotechnology , biology , engineering physics , engineering
The factors affecting myosin degradation that occurred during aging following high‐pressure treatment over a pressure range from 200 to 600 MPa were investigated by using SDS‐PAGE and immunoblotting analysis. The immunoblot pattern of myosin in muscle stored at 37°C for 48 h after pressure treatment at 0. 1 MPa (atmospheric pressure) or 200 MPa for 5 min was similar to that of native myosin incubated with cathepsin D, whereas at 400 or 600 MPa the pattern was close to that of native myosin incubated with cathepsin B. This phenomenon was reflected in the pressure‐susceptibilities of cathepsins B and D as reported in the literature (Homma and others 1994). However, these catheptic enzymes released by pressure treatment are unlikely to play a role in pressure‐induced tenderization of meat.