Antifreeze Activity of Surimi By-product Protein Hydrolysate and Its Cryoprotective Effect and Mechanism on Streptococcus thermophilus
In this study, the structure and antifreeze activity of surimi by-product protein hydrolysate (SBPH) were investigated, and the cryoprotective effect and mechanism on Streptococcus thermophilus were explored by measuring its growth performance, malondialdehyde (MDA) content, protease activity, metab...
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Format: | Article |
Language: | English |
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China Food Publishing Company
2023-04-01
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Series: | Shipin Kexue |
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Online Access: | https://www.spkx.net.cn/fileup/1002-6630/PDF/2023-44-7-005.pdf |
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author | ZHANG Xiaodi, DONG Ye, ZHANG Yiqi, DAI Zhiyuan |
author_facet | ZHANG Xiaodi, DONG Ye, ZHANG Yiqi, DAI Zhiyuan |
author_sort | ZHANG Xiaodi, DONG Ye, ZHANG Yiqi, DAI Zhiyuan |
collection | DOAJ |
description | In this study, the structure and antifreeze activity of surimi by-product protein hydrolysate (SBPH) were investigated, and the cryoprotective effect and mechanism on Streptococcus thermophilus were explored by measuring its growth performance, malondialdehyde (MDA) content, protease activity, metabolic activity and membrane potential after freezing treatment. The results showed that the molecular mass range of SBPH was 260–2 550 Da, and a total of 78 peptides with 8–18 amino residues were identified from SBPH, some of which had the characteristic structure of tripeptide repeat sequences imparting high antifreeze activity to SBPH (thermal hysteresis activity of 1.76 ℃). Compared with other antifreeze agents (sucrose, skim milk and glycerol), SBPH (2 mg/mL) enhanced the cell viability, growth activity and acid production of S. thermophilus after freezing treatment, attenuated oxidative stress damage to cells caused by low temperature, significantly inhibited the decrease in the relevant protease activity (P < 0.05), increased the metabolic activity of cells, and attenuated the hyperpolarization of the cell membrane thereby contributing to maintaining the integrity and fluidity of the cell membrane. SBPH could maintain the interaction between phospholipid bilayers to some extent and protect the structure of the cell membrane. In conclusion, SBPH can protect the function and integrity of cells, and reduce cryogenic damage to cells to a certain extent. |
first_indexed | 2024-03-13T05:55:16Z |
format | Article |
id | doaj.art-cf0eea5016a04b229722fd1e8e0947ac |
institution | Directory Open Access Journal |
issn | 1002-6630 |
language | English |
last_indexed | 2024-03-13T05:55:16Z |
publishDate | 2023-04-01 |
publisher | China Food Publishing Company |
record_format | Article |
series | Shipin Kexue |
spelling | doaj.art-cf0eea5016a04b229722fd1e8e0947ac2023-06-13T07:27:25ZengChina Food Publishing CompanyShipin Kexue1002-66302023-04-01447394710.7506/spkx1002-6630-20220407-085Antifreeze Activity of Surimi By-product Protein Hydrolysate and Its Cryoprotective Effect and Mechanism on Streptococcus thermophilusZHANG Xiaodi, DONG Ye, ZHANG Yiqi, DAI Zhiyuan0(1. Key Laboratory of Aquatic Products Processing of Zhejiang Province, Institute of Seafood, Zhejiang Gongshang University, Hangzhou 310035, China; 2. Collaborative Innovation Center of Seafood Deep Processing, Dalian 116000, China)In this study, the structure and antifreeze activity of surimi by-product protein hydrolysate (SBPH) were investigated, and the cryoprotective effect and mechanism on Streptococcus thermophilus were explored by measuring its growth performance, malondialdehyde (MDA) content, protease activity, metabolic activity and membrane potential after freezing treatment. The results showed that the molecular mass range of SBPH was 260–2 550 Da, and a total of 78 peptides with 8–18 amino residues were identified from SBPH, some of which had the characteristic structure of tripeptide repeat sequences imparting high antifreeze activity to SBPH (thermal hysteresis activity of 1.76 ℃). Compared with other antifreeze agents (sucrose, skim milk and glycerol), SBPH (2 mg/mL) enhanced the cell viability, growth activity and acid production of S. thermophilus after freezing treatment, attenuated oxidative stress damage to cells caused by low temperature, significantly inhibited the decrease in the relevant protease activity (P < 0.05), increased the metabolic activity of cells, and attenuated the hyperpolarization of the cell membrane thereby contributing to maintaining the integrity and fluidity of the cell membrane. SBPH could maintain the interaction between phospholipid bilayers to some extent and protect the structure of the cell membrane. In conclusion, SBPH can protect the function and integrity of cells, and reduce cryogenic damage to cells to a certain extent.https://www.spkx.net.cn/fileup/1002-6630/PDF/2023-44-7-005.pdfsurimi by-product; protein hydrolysate; streptococcus thermophiles; anti-freezing activity; action mechanism |
spellingShingle | ZHANG Xiaodi, DONG Ye, ZHANG Yiqi, DAI Zhiyuan Antifreeze Activity of Surimi By-product Protein Hydrolysate and Its Cryoprotective Effect and Mechanism on Streptococcus thermophilus Shipin Kexue surimi by-product; protein hydrolysate; streptococcus thermophiles; anti-freezing activity; action mechanism |
title | Antifreeze Activity of Surimi By-product Protein Hydrolysate and Its Cryoprotective Effect and Mechanism on Streptococcus thermophilus |
title_full | Antifreeze Activity of Surimi By-product Protein Hydrolysate and Its Cryoprotective Effect and Mechanism on Streptococcus thermophilus |
title_fullStr | Antifreeze Activity of Surimi By-product Protein Hydrolysate and Its Cryoprotective Effect and Mechanism on Streptococcus thermophilus |
title_full_unstemmed | Antifreeze Activity of Surimi By-product Protein Hydrolysate and Its Cryoprotective Effect and Mechanism on Streptococcus thermophilus |
title_short | Antifreeze Activity of Surimi By-product Protein Hydrolysate and Its Cryoprotective Effect and Mechanism on Streptococcus thermophilus |
title_sort | antifreeze activity of surimi by product protein hydrolysate and its cryoprotective effect and mechanism on streptococcus thermophilus |
topic | surimi by-product; protein hydrolysate; streptococcus thermophiles; anti-freezing activity; action mechanism |
url | https://www.spkx.net.cn/fileup/1002-6630/PDF/2023-44-7-005.pdf |
work_keys_str_mv | AT zhangxiaodidongyezhangyiqidaizhiyuan antifreezeactivityofsurimibyproductproteinhydrolysateanditscryoprotectiveeffectandmechanismonstreptococcusthermophilus |