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This study details the nutritional and digestive properties of protein isolates that are extracted from carp (Cyprinus Carpio L.) muscle using pH shifting methods. Alkaline (ALPI) and acid (ACPI) protein isolates exhibit higher protein yields (87.6%, 76.3%, respectively). In addition to the high recovery of myofibrillar protein, a portion of the water‐soluble proteins is also recovered. The moisture contents of ACPI and ALPI are 85.5% and 88.5%, respectively, and the crude protein contents of these two fractions are 83.20% and 83.0%, respectively, both contents of which are higher than those for fresh muscle. Most part of the ash and fat are removed in the separation process. The protein isolation is also found to be lighter and whiter than the fresh muscle and there is no difference between amino acid content of protein isolation and that of fresh muscle. The maximum solubility of water washed surimi is 73.21%, while solubility of ACPI‐2 and ALPI‐2 (pH 7.0) are 66.67% and 62.08%, respectively. The digestibility of ALPI and ACPI is improved after being treated with chymotrypsin, which is about 7–8 times as that of fresh muscle. The results indicate that the protein isolates have better nutritional and digestive properties than the fresh muscle does in food processing.Practical ApplicationsCommon carp is a lower additional value fish that exists in large amount in China. This study investigates nutritional and digestive properties of protein from carp extracted by pH shifting methods. According to the obtained data in this study, pH shifting method is a good protein recovery method that can effectively remove bone spurs, skin, fat and other impurities. In addition, sarcoplasmic proteins can also be recovered. The nutritional properties of protein isolates of carp were suitable for supplementing as an ingredient for human consumption. The pH‐shift process greatly improves the protein digestibility. Therefore, there are broad application prospects of the protein isolation as protein ingredients in food industry.

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The purpose of this study was to confirm inosine monophosphate (IMP) generation and to clarify the decomposition pathway of adenosine monophosphate (AMP) by investigating the properties of AMP, IMP, and adenosine (AdR) decomposition enzymes in Japanese scallop (Patinopecten yessoensis). The results showed that IMP accumulated due to AMP decomposition via endogenous enzymes in scallops stored at both 4 °C and 20 °C. The AMP decomposition rate was highest in the supernatant of homogenized scallop adductor muscle, followed by the suspended solution and precipitate, while IMP could not be decomposed in scallop. The results indicated that the activity of AdR deaminase was very high, and this enzyme was involved in an intracellular process in scallop. Moreover, 1 min of heating exerted little influence on the AMP and AdR decomposition rates, while 5 min of heating induced enzyme denaturation. The IMP generation rate increased dramatically in scallop crude enzyme solution containing 5 mM ethylenediaminetetraacetic acid (EDTA). This suggests that the major pathway of AMP decomposition might change with variations in metal ion concentrations in Japanese scallop.Practical ApplicationIMP generation in Japanese scallop (Patinopecten yessoensis) caused by endogenous enzymes was confirmed. IMP is very important for the umami taste (a pleasant savory taste) of aquatic products. As IMP accumulation might be achieved by changing the concentration of divalent metal ions and no IMP 5’‐nucleotidase activity was detected in scallop, a suitable process to produce good flavor scallops with high IMP contents might be developed.

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Three types of proteinases, namely cystein-, metallo-, and serine-proteinases were found in squid hepatopancreas by studying the inhibition spectra using carp myofibril as substrates. Cystein-, metallo-, and serine-type showed the highest activities at 50 ºC, 35 ºC, and 40 ºC, respectively. The optimal pHs were pH 5, pH 7, and pH 9 for cystein-, metallo-, and serine-type, respectively. When assayed at 20 ºC and pH7.5, metallo-type showed the highest activity. Metallo-type was characterized by a high selectivity in the digestion of myosin. Among the three enzymes, cystein-type was found to be the most stable against thermal and acid treatments. Heat treated myofibrils were more susceptible to cystein-and serine-types, but less susceptible to metallo-type. Acid treatment of myofibrils also enhanced the digestibility by cystein-type. The results indicated that cystein-type seemed to be the most suitable enzyme to produce peptides from denatured myofibrils by their random digestion.

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