Cryoprotective Activity of Different Characterized Fractions Isolated from Enzymatic Hydrolysates of Croceine Croaker (
In this study, ultrafiltration fractions (<3 k Da, LMH; >3 k Da, HMH) and solid-phase extraction fractions (hydrophilic hydrolysate, HIH; hydrophobic hydrolysate, HOH) from trypsin hydrolysate purified from croceine croaker (Pseudosciaena crocea) isolate were obtained to investigate the cryopr...
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Online Access: | https://doi.org/10.3390/foods13121946 https://pubmed.ncbi.nlm.nih.gov/38928887 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11202479/ |
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ftpubmed:38928887 2024-09-15T18:40:00+00:00 Cryoprotective Activity of Different Characterized Fractions Isolated from Enzymatic Hydrolysates of Croceine Croaker ( Xu, Zhe Cao, ShengAo Cui, Na Zhang, Rui Zhao, Shuang Zhang, Lijuan Guan, Shuang Xu, Yikun Yan, Xu Zhu, Zhixuan Tan, Zhijian Li, Tingting 2024 Jun 20 https://doi.org/10.3390/foods13121946 https://pubmed.ncbi.nlm.nih.gov/38928887 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11202479/ eng eng MDPI https://doi.org/10.3390/foods13121946 https://pubmed.ncbi.nlm.nih.gov/38928887 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11202479/ Foods ISSN:2304-8158 Volume:13 Issue:12 anti-freezing cryoprotective isolation myofibrillar protein trypsin hydrolysates Journal Article 2024 ftpubmed https://doi.org/10.3390/foods13121946 2024-06-29T16:02:00Z In this study, ultrafiltration fractions (<3 k Da, LMH; >3 k Da, HMH) and solid-phase extraction fractions (hydrophilic hydrolysate, HIH; hydrophobic hydrolysate, HOH) from trypsin hydrolysate purified from croceine croaker (Pseudosciaena crocea) isolate were obtained to investigate the cryoprotective effects of the different fractions, achieved by means of maceration of turbot fish meat after three freeze-thaw cycles. Alterations in the texture, color, moisture loss, myofibrillar protein oxidation stability and conformation, and microstructure of the fish were analyzed after freezing and thawing. The results demonstrate that HIH maximized the retention of fish texture, reduced moisture loss, minimized the oxidation and aggregation of myofibrillar proteins, and stabilized the secondary and tertiary structures of myofibrillar proteins compared to the control group. In conclusion, the HIH component in the trypsin hydrolysates of croceine croaker significantly contributes to minimizing freeze damage in fish meat and acts as an anti-freezing agent with high industrial application potential. Article in Journal/Newspaper Turbot PubMed Central (PMC) Foods 13 12 1946 |
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Open Polar |
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PubMed Central (PMC) |
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ftpubmed |
language |
English |
topic |
anti-freezing cryoprotective isolation myofibrillar protein trypsin hydrolysates |
spellingShingle |
anti-freezing cryoprotective isolation myofibrillar protein trypsin hydrolysates Xu, Zhe Cao, ShengAo Cui, Na Zhang, Rui Zhao, Shuang Zhang, Lijuan Guan, Shuang Xu, Yikun Yan, Xu Zhu, Zhixuan Tan, Zhijian Li, Tingting Cryoprotective Activity of Different Characterized Fractions Isolated from Enzymatic Hydrolysates of Croceine Croaker ( |
topic_facet |
anti-freezing cryoprotective isolation myofibrillar protein trypsin hydrolysates |
description |
In this study, ultrafiltration fractions (<3 k Da, LMH; >3 k Da, HMH) and solid-phase extraction fractions (hydrophilic hydrolysate, HIH; hydrophobic hydrolysate, HOH) from trypsin hydrolysate purified from croceine croaker (Pseudosciaena crocea) isolate were obtained to investigate the cryoprotective effects of the different fractions, achieved by means of maceration of turbot fish meat after three freeze-thaw cycles. Alterations in the texture, color, moisture loss, myofibrillar protein oxidation stability and conformation, and microstructure of the fish were analyzed after freezing and thawing. The results demonstrate that HIH maximized the retention of fish texture, reduced moisture loss, minimized the oxidation and aggregation of myofibrillar proteins, and stabilized the secondary and tertiary structures of myofibrillar proteins compared to the control group. In conclusion, the HIH component in the trypsin hydrolysates of croceine croaker significantly contributes to minimizing freeze damage in fish meat and acts as an anti-freezing agent with high industrial application potential. |
format |
Article in Journal/Newspaper |
author |
Xu, Zhe Cao, ShengAo Cui, Na Zhang, Rui Zhao, Shuang Zhang, Lijuan Guan, Shuang Xu, Yikun Yan, Xu Zhu, Zhixuan Tan, Zhijian Li, Tingting |
author_facet |
Xu, Zhe Cao, ShengAo Cui, Na Zhang, Rui Zhao, Shuang Zhang, Lijuan Guan, Shuang Xu, Yikun Yan, Xu Zhu, Zhixuan Tan, Zhijian Li, Tingting |
author_sort |
Xu, Zhe |
title |
Cryoprotective Activity of Different Characterized Fractions Isolated from Enzymatic Hydrolysates of Croceine Croaker ( |
title_short |
Cryoprotective Activity of Different Characterized Fractions Isolated from Enzymatic Hydrolysates of Croceine Croaker ( |
title_full |
Cryoprotective Activity of Different Characterized Fractions Isolated from Enzymatic Hydrolysates of Croceine Croaker ( |
title_fullStr |
Cryoprotective Activity of Different Characterized Fractions Isolated from Enzymatic Hydrolysates of Croceine Croaker ( |
title_full_unstemmed |
Cryoprotective Activity of Different Characterized Fractions Isolated from Enzymatic Hydrolysates of Croceine Croaker ( |
title_sort |
cryoprotective activity of different characterized fractions isolated from enzymatic hydrolysates of croceine croaker ( |
publisher |
MDPI |
publishDate |
2024 |
url |
https://doi.org/10.3390/foods13121946 https://pubmed.ncbi.nlm.nih.gov/38928887 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11202479/ |
genre |
Turbot |
genre_facet |
Turbot |
op_source |
Foods ISSN:2304-8158 Volume:13 Issue:12 |
op_relation |
https://doi.org/10.3390/foods13121946 https://pubmed.ncbi.nlm.nih.gov/38928887 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11202479/ |
op_doi |
https://doi.org/10.3390/foods13121946 |
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Foods |
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13 |
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12 |
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1946 |
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1810484333013630976 |