Enzymatic hydrolysis of starry triggerfish (Abalistes stellaris) muscle using liver proteinase from albacore tuna (Thunnus alalunga).

Proteinases from liver extract from albacore tuna (Thunnus alalunga) were used to produce protein hydrolysate from starry triggerfish (Abalistes stellaris) muscle. Hydrolysis conditions for preparing protein hydrolysate from starry triggerfish muscle were optimized. Enzyme level, reaction time and fish muscle/buffer ratio significantly affected the hydrolysis (p < 0.05). Optimum conditions for triggerfish muscle hydrolysis were 5.5 % liver extract, 40 min reaction time and fish muscle/buffer ratio of 1:3 (w/v). The freeze-dried protein hydrolysate was characterized with respect to chemical composition, amino acid composition and color. The product contained 91.73 % protein, 2.04 % lipid and 6.48 % ash. The protein hydrolysate exhibited high amount of essential amino acids (45.62 %). It was light yellow in color (L (*) = 82.94, a (*) = 0.84, b (*) = 22.83). The results indicate that the extract from liver of albacore tuna could be used to produce fish protein hydrolysate and protein hydrolysate from starry triggerfish muscle may potentially serve as a good source of desirable peptide and amino acids.

Interaction of fish myoglobin and myofibrillar proteins.

Interactions between fish myoglobin (Mb) and myofibrillar proteins were investigated in a Mb-natural actomyosin (NAM) model at 4 degrees C. Increases in metmyoglobin (MetMb) formation and the relative content of bound Mb were observed, as were decreases in whiteness and Ca(2+)-ATPase activity (P < 0.05). During the first 6 h of incubation, Mb bound preferably to myosin at domains other than the head portion, as evidenced by measurable ATPase activity. The potential binding of Mb to myosin heads occurred after 24-h incubation as evidenced by the marked decrease in Ca(2+)-ATPase activity of the NAM-Mb mixture when compared to that of NAM alone (P < 0.05). The interaction between fish Mb and myofibrillar proteins was more pronounced with increased storage time; formation of high-molecular-weight aggregates (> 206 kDa) also increased with time. Electrophoretic study revealed that disulfide bonds were not involved in Mb-NAM interactions.

Discoloration and lipid deterioration of farmed giant catfish (Pangasianodon gigas) muscle during refrigerated storage.

Discoloration and lipid deterioration of farmed giant catfish (Pangasianodon gigas) muscle during 14 d refrigerated storage were investigated. Lipid deterioration, lipolysis, and lipid oxidation in both dorsal and ventral muscles increased as storage time increased. A progressive formation of primary lipid oxidation products monitored by the increase in conjugated dienes (CD) was observed (P < 0.05) and the increase in thiobarbituric reactive substances (TBARS), an index of secondary lipid oxidation products, was noticeable throughout the storage (P < 0.05). The pH of both dorsal and ventral muscles tended to increase as storage time continued (P < 0.05). A gradual increase in free fatty acid (FFA) formation was found within the first 10 d of refrigerated storage (P < 0.05), suggesting hydrolysis induced by lipases and phospholipases. However, a sharp decrease in FFA content was observed at the end of storage. Refrigerated storage also resulted in changes in redness index of both dorsal and ventral muscles. These changes were coincidental with the changes in metmyoglobin content. Therefore, the discoloration and lipid changes in giant catfish muscle during refrigerated storage depended on the muscle type and might be related to the difference in composition between dorsal and ventral muscles.

Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins.

The effects of ionic strength (0, 0.3, and 0.6 M KCl) and temperature (4 and 25 degrees C) on the interaction between fish myoglobin and myofibrillar proteins were investigated in a model system. Increases in the relative content of bound myoglobin and metmyoglobin formation in myoglobin-natural actomyosin (NAM) mixtures with concurrent decreases in whiteness and Ca(2+)-ATPase activity were observed with increasing ionic strength (P < 0.05). The relative content of bound myoglobin and the oxidation of oxymyoglobin were generally greater at 25 degrees C than at 4 degrees C (P < 0.05). Binding of myoglobin to NAM resulted in decreased whiteness (P < 0.05). Ca(2+)-ATPase was not affected by temperature (P > 0.05). SDS-PAGE patterns of protein samples suggested that myoglobin-NAM interactions did not involve disulfide bonds. The formation of high-molecular-weight aggregates (>206 kDa) was observed and was more pronounced at higher ionic strength and higher temperature.