The changes of actomyosin, proteolytic activities and myofibril fragmentation during the postmortem aging of grass carp were studied. The study revealed dramatically increased actomyosin dissociation within 6 h of storage postmortem in grass carp, and it was associated with the drop of pH from 6.9 to 6.7, while liberated actin remained almost unchanged after 6 h postmortem. The myofibril fragmentation also increased significantly with the storage time in 6 h, and a highly positive correlation (P<0.01) existed between MFI and cathepsin B, D, H activities. The study indicated both actomyosin dissociation and cathepsin B, D, H played a role in postmortem tenderization and textural changes in grass carp.
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http://dx.doi.org/10.1016/j.foodchem.2015.10.132 | DOI Listing |
Objective: Aim: To determine the profound inf l uence of scorpion venom toxins on the intricate structure of the heart of mammals, a topic of utmost importance in toxicology and cardiovascular health.
Patients And Methods: Materials and Methods: A meticulous and comprehensive literature analysis was conducted using PubMed, Google Scholar, Web of Science, and Scopus databases. We meticulously selected the newest publications up to 5 years old or the most thorough publications that vividly described our topic's essence, ensuring our findings' credibility and reliability.
Foods
October 2024
Department of Food Science, Guangxi University, Nanning 530004, China.
Water-free transportation (WFT) causes shrimp () flesh quality deterioration. However, the roles of endogenous protease-induced protein hydrolysis have been neglected in the research. In the present study, calpain zymography, gelatinase zymography, the hematoxylin-eosin staining method, and other methods were applied to investigate the response of various endogenous proteases (cathepsin, calpain, and gelatinase), the myofibril fragmentation index (MFI), and the microscopic morphology of shrimp muscle during WFT in comparison with the shrimp under the conventional water transportation strategy (WT).
View Article and Find Full Text PDFChemical analysis showed that pH, values, myosin turbidity, carbonyl content, and surface hydrophobicity elevated in hooked, trawl-net, and radar-net hairtail (, HH, TH, and RH) muscles with the prolonged cryopreservation time (-18℃, 120 d). In contrast, , values, textural properties, and myosin solubility existed decreasing trends. Microstructural results showed that freezing resulted in disordered myofibrils, decreased collagen fibers, widened myofibrillar space, and increased fragmentation in hairtail muscles.
View Article and Find Full Text PDFCommun Biol
October 2024
Department of Pathology, Emory University, Atlanta, GA, USA.
UNC-89 is a giant sarcomeric M-line protein required for sarcomere organization and optimal muscle function. UNC-89 contains two protein kinase domains, PK1 and PK2, separated by an elastic region. Here we show that PK2 is a canonical kinase expected to be catalytically active.
View Article and Find Full Text PDFJ Biol Chem
November 2024
Nano Medical Engineering Laboratory, Cluster for Pioneering Research, RIKEN, Wako, Japan; Emergent Bioengineering Materials Research Team, Center for Emergent Matter Science, RIKEN, Wako, Japan.
Intracellular calcium dynamics is key to regulating various physiological events. Myotube formation by myoblast fusion is controlled by the release of Ca from the endoplasmic reticulum (ER), and the calpain (CAPN) family is postulated to be an executioner of the process. However, the activation of a specific member of the family or its physiological substrates is unclear.
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