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Properties of Proteolytic Enzymes from Muscle of Octopus ( Octopus vulgaris ) and Effects of High Hydrostatic Pressure
Author(s) -
Hurtado J.L.,
Montero P.,
Borderías J.,
An H.
Publication year - 2002
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.1365-2621.2002.tb08776.x
Subject(s) - octopus (software) , autolysis (biology) , myofibril , hydrostatic pressure , biochemistry , enzyme , proteolytic enzymes , chemistry , cysteine , cathepsin , biology , serine , physics , computational chemistry , thermodynamics
The proteolytic activity of octopus arm muscle exhibited optimum activity at 40°C and 60°C, at optimum pH 2.5 and 4.0, respectively. The proteinases were inhibited strongly by cysteine‐ and aspartic‐proteinase inhibitors and, to a lesser degree, by serine‐proteinase inhibitors at 40°C, and by cysteine‐proteinase inhibitors at 60°C. High pressure did not modify the temperature and pH autolytic activity profiles. The autolytic activity at 40°C was reduced by high pressure; however, it was increased at an incubation temperature of 60°C, mainly in muscle pressurized at 7°C. Aspartic‐proteinase was the most sensitive to high pressure. The autolysis of myofibrillar proteins was reduced by high pressure, which was evident in MHC band.