Studies on the Comparison of Component Composition and Biological Function of Peptides from Mollusk

• Main Author: 林澄治
• Other Authors: 曹欽玉
• Format: Others
• Language: zh-TW
• Published: 1999
• Online Access: http://ndltd.ncl.edu.tw/handle/75798275088660176466

碩士 === 國立海洋大學 === 食品科學系 === 87 === Mollusk is an important resources of fishery harvest. There are a few reports on this aspect, peptide in mollusk extractives. Therefore, the mollusks have the potential development in the future. To investigate and compare the pattern of different molecular weight, amino acid composition and biological function of peptide from mollusk. Some species of bivales, gastropoda and cephalopods were used in the studies. The water extractive of each sample was chromatographied on Sephadex G-25 column to obtain the different molecular weight of peptides. Each peptide peak fractionation was collected and observed its biological function by using glycolytic, proteolytic and metabolic enzymes. It was found that the muscle extractives of Sinonovacula constricta and Ruditapes variegatus have very strong inhibition on α-amylase activity; Babylonia areolata have inhibiting ability of trypsin activity; Haliotis aquatilis have the inhibition ability of papain activity; Tegula argyrostoma and Loligo edulis Hoyle have activating theα-amylase activity; Haliotis aquatilis has activating chymotrypsin activity; Babylonia areolata and Octopus variabilis have the activators of malic enzyme activity, and the entrail extractives of Ruditapes variegatus and Babylonia areolata have inhibiting the α-amylase activity; Octopus variabilis has inhibiting the chymotrypsin activity; Octopus variabilis and Loligo edulis Hoyle have the inhibitor of papain activity; Haliotis aquatilis, Tegula argyrostoma and Octopus variabilis have activating α-amylase activity; Haliotis aquatilis has the activator of malic enzyme activity. The peptides affecting the enzyme activity aren''t limited the MW size, source and the same amino acid composition.Group I(Val, Cys, Met, Leu and Lys)and group II(Val, Cys and Met) maybe forming an unique structure respectively.Theα-amylase activity can be activated by the former and inhibited by the later.