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Properties of proteolytic enzymes from muscle of octopus (Octopus vulgaris) and effects of high hydrostatic pressure

AuthorsHurtado, José L.; Montero García, Pilar ; Borderías, A. Javier ; An, H.
Issue Date2002
PublisherInstitute of Food Technologists
CitationJournal of Food Science 67: 2555- 2564 (2002)
AbstractThe 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.
Identifiersissn: 0022-1147
Appears in Collections:(IF) Artículos
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