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Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze–Thaw Cycles

Whey protein hydrolysate (WPH) has made a breakthrough in inhibiting oxidative deterioration and improving the quality of meat products during storage. Based on our previous study of extracting the most antioxidant active fraction I (FI, the molecular weight < 1 kDa) from whey protein hydrolysate...

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Autores principales: Yu, Pengjuan, Yan, Jiayan, Kong, Lingru, Yu, Juan, Zhao, Xinxin, Peng, Xinyan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10453259/
https://www.ncbi.nlm.nih.gov/pubmed/37628134
http://dx.doi.org/10.3390/foods12163135
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author Yu, Pengjuan
Yan, Jiayan
Kong, Lingru
Yu, Juan
Zhao, Xinxin
Peng, Xinyan
author_facet Yu, Pengjuan
Yan, Jiayan
Kong, Lingru
Yu, Juan
Zhao, Xinxin
Peng, Xinyan
author_sort Yu, Pengjuan
collection PubMed
description Whey protein hydrolysate (WPH) has made a breakthrough in inhibiting oxidative deterioration and improving the quality of meat products during storage. Based on our previous study of extracting the most antioxidant active fraction I (FI, the molecular weight < 1 kDa) from whey protein hydrolysates of different molecular weights, the present study continued to delve into the effects of WPH with fraction I on the structure and function of myofibrillar proteins (MP) in ground pork during the freeze–thaw (F-T) cycles. With the number of F-T cycles raised, the total sulfhydryl content, the relative contents of α-helix, Ca(2+)-ATPase activity, K(+)-ATPase activity, solubility, emulsion activity index (EAI), and emulsion stability index (ESI) of MP gradually decreased. Conversely, the carbonyl content and the relative content of random curl showed an increasing trend. In particular, the damage to the structure and the function of MP became more pronounced after three F-T cycles. But, during F-T cycles, FI stabilized the structure of MP. Compared to the control group, the 10% FI group showed a remarkable improvement (p < 0.05) in the total sulfhydryl content, Ca(2+)-ATPase activity, K(+)-ATPase activity, solubility, EAI and ESI after multiple F-T cycles, suggesting that 10% FI could effectively inhibit protein oxidation and had the influence of preserving MP function properties. In conclusion, WPH with fraction I can be used as a potential natural antioxidant peptide for maintaining the quality of frozen processed meat products.
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spelling pubmed-104532592023-08-26 Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze–Thaw Cycles Yu, Pengjuan Yan, Jiayan Kong, Lingru Yu, Juan Zhao, Xinxin Peng, Xinyan Foods Article Whey protein hydrolysate (WPH) has made a breakthrough in inhibiting oxidative deterioration and improving the quality of meat products during storage. Based on our previous study of extracting the most antioxidant active fraction I (FI, the molecular weight < 1 kDa) from whey protein hydrolysates of different molecular weights, the present study continued to delve into the effects of WPH with fraction I on the structure and function of myofibrillar proteins (MP) in ground pork during the freeze–thaw (F-T) cycles. With the number of F-T cycles raised, the total sulfhydryl content, the relative contents of α-helix, Ca(2+)-ATPase activity, K(+)-ATPase activity, solubility, emulsion activity index (EAI), and emulsion stability index (ESI) of MP gradually decreased. Conversely, the carbonyl content and the relative content of random curl showed an increasing trend. In particular, the damage to the structure and the function of MP became more pronounced after three F-T cycles. But, during F-T cycles, FI stabilized the structure of MP. Compared to the control group, the 10% FI group showed a remarkable improvement (p < 0.05) in the total sulfhydryl content, Ca(2+)-ATPase activity, K(+)-ATPase activity, solubility, EAI and ESI after multiple F-T cycles, suggesting that 10% FI could effectively inhibit protein oxidation and had the influence of preserving MP function properties. In conclusion, WPH with fraction I can be used as a potential natural antioxidant peptide for maintaining the quality of frozen processed meat products. MDPI 2023-08-21 /pmc/articles/PMC10453259/ /pubmed/37628134 http://dx.doi.org/10.3390/foods12163135 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Yu, Pengjuan
Yan, Jiayan
Kong, Lingru
Yu, Juan
Zhao, Xinxin
Peng, Xinyan
Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze–Thaw Cycles
title Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze–Thaw Cycles
title_full Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze–Thaw Cycles
title_fullStr Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze–Thaw Cycles
title_full_unstemmed Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze–Thaw Cycles
title_short Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze–Thaw Cycles
title_sort whey protein hydrolysate improved the structure and function of myofibrillar protein in ground pork during repeated freeze–thaw cycles
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10453259/
https://www.ncbi.nlm.nih.gov/pubmed/37628134
http://dx.doi.org/10.3390/foods12163135
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