Dataset Information

Effect of Lysosomal Cathepsin L on Proteolysis of Beef Myofibrillar Proteins In Vivo and In Vitro.

ABSTRACT: This study investigated the effects of cathepsin L on proteolysis of beef myofibrillar proteins in vivo and in vitro. Results indicated that cathepsin L affected the degradation of desmin and troponin-T during postmortem aging, and the extent of degradation increased from 1 d to 14 d postmortem. No detectable degradation of titin, nebulin, and α-actinin in the presence of cathepsin L inhibitor was observed during postmortem aging. In vitro, cathepsin L affected the degradation of titin, nebulin, and troponin-T, and the extent of degradation increased with increasing incubation time. Nevertheless, cathepsin L did not cause the degradation of α-actinin and desmin, regardless of incubation temperature. The different results between in vitro and in vivo experiments might mainly depend on different treatment temperatures. Overall, these results indicated that cathepsin L participated in the degradation of myofibrillar proteins and meat tenderization.

SUBMITTER: Cui B

PROVIDER: S-EPMC8871152 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature

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Effect of Lysosomal Cathepsin L on Proteolysis of Beef Myofibrillar Proteins In Vivo and In Vitro.

Cui Baowei B Guo Xiuyun X Zhang Yawei Y Meng Xiangren X

Foods (Basel, Switzerland) 20220221 4

This study investigated the effects of cathepsin L on proteolysis of beef myofibrillar proteins in vivo and in vitro. Results indicated that cathepsin L affected the degradation of desmin and troponin-T during postmortem aging, and the extent of degradation increased from 1 d to 14 d postmortem. No detectable degradation of titin, nebulin, and α-actinin in the presence of cathepsin L inhibitor was observed during postmortem aging. In vitro, cathepsin L affected the degradation of titin, nebulin, ...[more]

PMID: 35206088

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Project description:Tenderness is an important sensory attribute to the overall eating experience of beef. Identifying novel methods to ensure consistent tenderness, especially in inherently tough cuts, is critical for the industry. This study investigated if tumbling without brine inclusion could be an effective method to improve the quality and palatability attributes of beef longissimus lumborum (LL) and semitendinosus (ST) steaks. Furthermore, interactions with postmortem aging were evaluated to determine how tumbling might affect protein degradation and muscle ultrastructure. At 5 d postmortem, pairs of LL and ST muscles from beef carcasses (n = 16) were bisected, vacuum packaged, and tumbled for 0, 40, 80, or 120 min. Sections were divided and subsequently aged an additional 0 or 10 d at 2 °C. Tumbling for any duration improved instrumental tenderness of LL (P < 0.001) but not ST (P > 0.05) steaks, regardless of aging time. Tumbling exacerbated moisture loss in both muscles shown by greater purge and cooking losses (P < 0.05). Myofibrillar fragmentation was induced through tumbling in both muscles (P < 0.001), which was supported by transmission electron microscopy images. Tumbling for 120 min followed by 10 d of aging resulted in less abundant intact troponin-T in both LL and ST (P < 0.05), as well as less intact desmin in ST (P < 0.05); however, calpain-1 autolysis was not affected by tumbling (P > 0.05). No effects of tumbling, aging, nor the interaction were found for the content and solubility of collagen (P > 0.05). Consumer panelists (n = 120/muscle) rated LL steaks tumbled for any duration higher for tenderness and overall liking compared to control steaks (P < 0.05). For ST, significant interactions were found for consumer liking of tenderness and juiciness. In general, tumbling without subsequent aging resulted in poorer juiciness than non-tumbled (P < 0.05), while at 10 d no differences in juiciness were found between treatments (P > 0.05). For ST steaks that were aged 10 d, 120 min of tumbling resulted in greater tenderness liking than non-tumbled steaks (P < 0.05). These results suggest that tumbling would result in myofibrillar fragmentation and may benefit the degradation of myofibrillar proteins; however, there would be negligible impacts on collagen. Accordingly, tumbling without brine inclusion alone may be sufficient to improve tenderness and overall liking of LL steaks, while combined tumbling with subsequent postmortem aging would be necessary to improve tenderness liking of ST.

Dataset Information

Effect of Lysosomal Cathepsin L on Proteolysis of Beef Myofibrillar Proteins In Vivo and In Vitro.

Publications

Effect of Lysosomal Cathepsin L on Proteolysis of Beef Myofibrillar Proteins In Vivo and In Vitro.

Similar Datasets

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