Properties of Proteolytic Enzymes from Muscle of Octopus (Octopus vulgaris) and Effects of High Hydrostatic Pressure
Hurtado, J.L. ; Montero, P. ; Borderías, J. ; An, H.
Oxford, UK : Blackwell Publishing Ltd
Published 2002
Oxford, UK : Blackwell Publishing Ltd
Published 2002
| ISSN: |
1750-3841
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| Source: |
Blackwell Publishing Journal Backfiles 1879-2005
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| Topics: |
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
Process Engineering, Biotechnology, Nutrition Technology
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| Notes: |
: 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.
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| Type of Medium: |
Electronic Resource
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| URL: |