Effect of Low Temperature Plasma Sterilization on Myosin Degradation and Related Cathepsin Activity of Oncorhynchus mykiss
To clarify the mechanism of the effect of low temperature plasma sterilization on the degradation of Oncorhynchus mykiss and related cathepsin activity, Oncorhynchus mykiss fillets were treated with 70 kV dielectric barrier discharge low temperature plasma (DBD) sterilization and storage under ice t...
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The editorial department of Science and Technology of Food Industry
2025-06-01
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| Series: | Shipin gongye ke-ji |
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| author | Xiejun SUN Xiaoqiao CHEN Xiuxia LI Jianrong LI |
| author_facet | Xiejun SUN Xiaoqiao CHEN Xiuxia LI Jianrong LI |
| author_sort | Xiejun SUN |
| collection | DOAJ |
| description | To clarify the mechanism of the effect of low temperature plasma sterilization on the degradation of Oncorhynchus mykiss and related cathepsin activity, Oncorhynchus mykiss fillets were treated with 70 kV dielectric barrier discharge low temperature plasma (DBD) sterilization and storage under ice temperature for 8 d. Changes in texture, TCA soluble peptides, amino acid nitrogen, myofibrillar fragmentation index (MFI) of Oncorhynchus mykiss fillets from different storage days were analyzed, and the activities of cathepsin B, D, and L in the fillets and their degradation effects on myosin were explored. The binding of the main active substance NO3− produced by DBD sterilization with cathepsin was further analyzed through molecular dynamics simulation. The results showed that 70 kV DBD treatment had no significant effect on the hardness and elasticity of Oncorhynchus mykiss fillets during early storage (P>0.05), and the reduction of hardness and elasticity was delayed during the storage. It also delayed the increase of TCA soluble peptides, myofibrillar fragmentation index (MFI), and amino acid nitrogen content. The activity of cathepsins B and L were significantly inhibited (P<0.05), and the degradation of myosin light chain MLC-2 fragment was slowed. The activity of cathepsin B, D and L was significantly reduced after DBD sterilization (P<0.05). Molecular dynamics simulations showed that the binding free energies of cathepsin B, D and L with NO3− were −10.937, −5.0555, and −19.112 kcal/mol, respectively, and the hydrogen bonding frequencies of cathepsin B, D, and L with NO3− were 13.56%, 15.02%, and 31.23%, respectively, indicating stronger hydrogen bonding between NO3− and cathepsin L. The degradation of fish protein and activity of cathepsin could be delayed by DBD sterilization, and the texture of fish fillet was maintained. The greatest effect on cathepsin L was shown by the active ingredient NO3− produced by DBD sterilization, which could exist in a stable way in its active center and had low binding free energy. |
| format | Article |
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| institution | OA Journals |
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| language | zho |
| publishDate | 2025-06-01 |
| publisher | The editorial department of Science and Technology of Food Industry |
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| spelling | doaj-art-9cc8c765d24046579c736d2e384ebccf2025-08-20T02:35:32ZzhoThe editorial department of Science and Technology of Food IndustryShipin gongye ke-ji1002-03062025-06-014612505910.13386/j.issn1002-0306.20240601812024060181-12Effect of Low Temperature Plasma Sterilization on Myosin Degradation and Related Cathepsin Activity of Oncorhynchus mykissXiejun SUN0Xiaoqiao CHEN1Xiuxia LI2Jianrong LI3College of Food Science and Technology, Bohai University, National & Local Joint Engineering Research Center for Storage, Processing and Safety Control Technology of Fresh Agricultural Products, Jinzhou 121013, ChinaCollege of Food Science and Technology, Bohai University, National & Local Joint Engineering Research Center for Storage, Processing and Safety Control Technology of Fresh Agricultural Products, Jinzhou 121013, ChinaCollege of Food Science and Technology, Bohai University, National & Local Joint Engineering Research Center for Storage, Processing and Safety Control Technology of Fresh Agricultural Products, Jinzhou 121013, ChinaCollege of Food Science and Technology, Bohai University, National & Local Joint Engineering Research Center for Storage, Processing and Safety Control Technology of Fresh Agricultural Products, Jinzhou 121013, ChinaTo clarify the mechanism of the effect of low temperature plasma sterilization on the degradation of Oncorhynchus mykiss and related cathepsin activity, Oncorhynchus mykiss fillets were treated with 70 kV dielectric barrier discharge low temperature plasma (DBD) sterilization and storage under ice temperature for 8 d. Changes in texture, TCA soluble peptides, amino acid nitrogen, myofibrillar fragmentation index (MFI) of Oncorhynchus mykiss fillets from different storage days were analyzed, and the activities of cathepsin B, D, and L in the fillets and their degradation effects on myosin were explored. The binding of the main active substance NO3− produced by DBD sterilization with cathepsin was further analyzed through molecular dynamics simulation. The results showed that 70 kV DBD treatment had no significant effect on the hardness and elasticity of Oncorhynchus mykiss fillets during early storage (P>0.05), and the reduction of hardness and elasticity was delayed during the storage. It also delayed the increase of TCA soluble peptides, myofibrillar fragmentation index (MFI), and amino acid nitrogen content. The activity of cathepsins B and L were significantly inhibited (P<0.05), and the degradation of myosin light chain MLC-2 fragment was slowed. The activity of cathepsin B, D and L was significantly reduced after DBD sterilization (P<0.05). Molecular dynamics simulations showed that the binding free energies of cathepsin B, D and L with NO3− were −10.937, −5.0555, and −19.112 kcal/mol, respectively, and the hydrogen bonding frequencies of cathepsin B, D, and L with NO3− were 13.56%, 15.02%, and 31.23%, respectively, indicating stronger hydrogen bonding between NO3− and cathepsin L. The degradation of fish protein and activity of cathepsin could be delayed by DBD sterilization, and the texture of fish fillet was maintained. The greatest effect on cathepsin L was shown by the active ingredient NO3− produced by DBD sterilization, which could exist in a stable way in its active center and had low binding free energy.http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2024060181low temperature plasma sterilizationoncorhynchus mykissmyosincathepsintexture |
| spellingShingle | Xiejun SUN Xiaoqiao CHEN Xiuxia LI Jianrong LI Effect of Low Temperature Plasma Sterilization on Myosin Degradation and Related Cathepsin Activity of Oncorhynchus mykiss Shipin gongye ke-ji low temperature plasma sterilization oncorhynchus mykiss myosin cathepsin texture |
| title | Effect of Low Temperature Plasma Sterilization on Myosin Degradation and Related Cathepsin Activity of Oncorhynchus mykiss |
| title_full | Effect of Low Temperature Plasma Sterilization on Myosin Degradation and Related Cathepsin Activity of Oncorhynchus mykiss |
| title_fullStr | Effect of Low Temperature Plasma Sterilization on Myosin Degradation and Related Cathepsin Activity of Oncorhynchus mykiss |
| title_full_unstemmed | Effect of Low Temperature Plasma Sterilization on Myosin Degradation and Related Cathepsin Activity of Oncorhynchus mykiss |
| title_short | Effect of Low Temperature Plasma Sterilization on Myosin Degradation and Related Cathepsin Activity of Oncorhynchus mykiss |
| title_sort | effect of low temperature plasma sterilization on myosin degradation and related cathepsin activity of oncorhynchus mykiss |
| topic | low temperature plasma sterilization oncorhynchus mykiss myosin cathepsin texture |
| url | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2024060181 |
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