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Intestinal content accelerates muscle protein degradation in red shrimp (Solenocera crassicornis) during refrigeration: Insights from metagenomics and metabolomics.

This study systematically explored the effects of intestinal components on muscle quality deterioration and protein degradation of red shrimp during refrigerated storage. The results demonstrated that refrigeration induced continuous quality degradation and muscle protein breakdown in red shrimp, whereas eliminating intestinal tissues effectively retarded muscle spoilage and protein degradation, and optimized muscle texture. The intestinal microorganisms could secrete extracellular proteases to promote muscle protein degradation were primarily Vibrio, Bacillus, Pseudomonas, Photobacterium, and Shewanella. These microorganisms promote protein degradation by secreting zinc proteases, serine proteases, and aspartyl proteases. This study elucidates the molecular mechanisms of intestinal microbial metabolism influences the muscle protein degradation of red shrimp during refrigeration. The findings provide a theoretical foundation for precise regulation of intestinal-targeted microorganisms, thereby maintaining optimal quality of shrimps during refrigeration.

Animals

Structure-function studies on red pigment-concentrating hormone, II. The significance of the C-terminal tryptophan amide.

The significance of the C-terminal tryptophan residue of the red pigment-concentrating hormone (RPCH: Glu-Leu-Asn-Phe-Ser-Pro-Gly-Trp-NH2) regulating the blanching of the crustacean chromatophores has been investigated. RPCH and a number of analogues that differ only in the C-terminal part of the hormone, have been synthesized and assayed for biological activity on the shrimp Leander adspersus. It has been shown that the indole skeleton of tryptophan is an absolute requirement for the biological activity of the hormone. To provide maximum response the tryptophan must be blocked as the amide. The activity of synthetic [Tyr4]RPCH and adipokinetic hormone (AKH) purified from Schistocerca gregaria has been compared with the activity of synthetic RPCH.

Amides

Structure-function studies on red pigment-concentrating hormone; the significance of the terminal residues.

The significance of the terminal residues of the red pigment-concentrating hormone (RPCH: Glu-Leu-Asn-Phe-Ser-Pro-Gly-Trp-NH2) for its blanching effect on crustacean chromatophores has been investigated. The chemical synthesis of the following small analogues, starting from the C-terminal amino acid are described: Ac-Trp-NH2, Boc-Gly-Trp-NH2, Ac-Gly-Trp-NH2, Gly-Trp-NH2, Ac-Pro-Gly-Trp-NH2, Glu-Trp-NH2, Glu-Pro-Gly-Trp-NH2, Ac-Pro-Gly and Glu-Pro-Gly-NH2. Assay of the biological activity of the various synthetic compounds in the shrimp Leander adspersus has established that only the C-terminal tryptophan residue is indispensable for the blanching effect of the hormone, although elongation of the chain length improves its potency.

Animals