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SURFACE ULTRASTRUCTURE AND TENSILE PROPERTIES OF CATHEPSIN AND COLLAGENASE TREATED MUSCLE FIBERS
Author(s) -
EINO M. F.,
STANLEY D. W.
Publication year - 1973
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.1365-2621.1973.tb02773.x
Subject(s) - myofibril , ultrastructure , ultimate tensile strength , collagenase , cathepsin , elongation , breakage , sarcolemma , breaking strength , chemistry , biophysics , anatomy , swelling , materials science , composite material , biochemistry , biology , enzyme , membrane
Beef and rabbit psoas muscle fibers were soaked in a crude muscle cathepsin preparation, collagenase or 2% KCl. Tensile properties (breaking strength and break elongation) and surface ultrastructure were monitored. Cathepsins considerably accelerated decreases in tensile properties found in an un‐soaked control while KC1 produced significant but less extreme effects. Collagenase showed similar results for breaking strength but break elongation was only slightly influenced. Surface ultrastructure revealed that KC1 caused a variable loss of structure including collapse and disappearance of striations, swelling and some transverse fiber breakage. Cathepsins speeded and expanded this damage producing multiple breakage with extensive disruption in some cases. These effects are similar to those observed in naturally aged meat and occur at the same temperature and pH. Collagenase treatment, however, initially brought about a shredding and dissolution of collagen fibers followed by disintegration of the sarcolemma and exposure of relatively undamaged myofibrils.