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By Fereidoon Shahidi, J.R. Botta
This ebook examines chemical approaches and interactions present in seafood and discusses the processing recommendations used, with regards to caliber and sensory review. The processing and use of seafood by-products is usually lined.
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Extra resources for Seafoods: Chemistry, Processing Technology and Quality
Sample text
1986). 4 Cathepsin D. 23) is an endopeptidase having pepsin-like activity with protein substrates but differs from pepsin in its activity with low molecular weight substrates. 5. e. , 1981). Invertebrates secrete cathepsin D in the hepatopancreas and appear to use the enzyme in digestion. Gildberg (1988) suggests an evolutionary progression of cathepsin D, fish pepsin I, fish pepsin II and mammalian pepsin. , 1984a). , 1986). , 1987). , 1982b) and squid (Sakai and Matsumoto, 1981). Gildberg (1988) reviewed the comparative properties of invertebrate, fish and mammalian cathepsin D and concluded there are no apparent differences.
1979) Studies on fish muscle protease-VlI. On the existence of protease active in neutral pH range. Bull. lap. Soc. Sci. , 42, 665-70. , Hirotsuka, M. A. (1979) Neutral proteinase of carp muscle. l. , 44, 111 1986) J. Bioi. , 261, 9465. T. F. (1983) Proteolytic activities in the sarcoplasmic fluids of parasitized Pacific whiting (Merluccius productus) and unparasitized true cod (Gadus macrocephalus). 1. , 48,1315-19. B. 1. (1988) Multicatalytic proteinase in fish muscle. Arch. Biochem. , 267, 599-605. B. 1. (1989) Fish skeletal muscle contains a novcl serine proteinase with an unusual subunit composition. Biochem. , 263, 471-5. S. (1960) Cathepsins, in The Enzymes, (ed. D. Boyer, H. Lardy & K. Myrback).