High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution

Xing Chen; Youling L. Xiong; Xinglian Xu

doi:10.1016/j.foodchem.2019.01.131

High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution

Xing Chen, Youling L. Xiong, Xinglian Xu

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

62 Scopus citations

Abstract

This study tested the potential of high-pressure homogenization (HPH, 69 MPa) combined with hydrogen peroxide (H ₂ O ₂ , at 0, 40, 80, 160 and 320 μmol/g protein) on enhancing the stability of myofibrillar protein (MP, 15 mg/mL) against thermal aggregation (95 °C for 10 min) in aqueous solution. The addition of H ₂ O ₂ blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of H ₂ O ₂ by disrupting the intact myofibril structure and exposing buried –SH groups, and this resultedin stronger inhibition of thermal aggregation therefore improved solubility of MP. More than 75% of heated MP remained soluble after the treatment with HPH and 160 μmol/g H ₂ O ₂ , while untreated samples formed a gel upon heating. These results proved that HPH combined with H ₂ O ₂ is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.

Original language	English
Pages (from-to)	31-38
Number of pages	8
Journal	Food Chemistry
Volume	285
DOIs	https://doi.org/10.1016/j.foodchem.2019.01.131
State	Published - Jul 1 2019

Bibliographical note

Funding Information:
This study was supported by the National Key R&D Program of China (No. 2018YFD0401203 ), the USDA National Institute of Food and Agriculture (Hatch Project 1005724), the National Natural Science Foundation of China (No. 31671875 ), an Oversea Study Fellowship from the China Scholarship Council (to Xing Chen), and the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD). Approved for publication as journal article no. 18-07-008 by the Director of the Kentucky Agricultural Experiment Station.

Publisher Copyright:
© 2019 Elsevier Ltd

Keywords

Heat stability
High-pressure homogenization
Hydrogen peroxide
Myofibrillar protein
Protein beverage
Sulfhydryl blockage

ASJC Scopus subject areas

Analytical Chemistry
Food Science

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10.1016/j.foodchem.2019.01.131

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title = "High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution",

abstract = " This study tested the potential of high-pressure homogenization (HPH, 69 MPa) combined with hydrogen peroxide (H 2 O 2 , at 0, 40, 80, 160 and 320 μmol/g protein) on enhancing the stability of myofibrillar protein (MP, 15 mg/mL) against thermal aggregation (95 °C for 10 min) in aqueous solution. The addition of H 2 O 2 blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of H 2 O 2 by disrupting the intact myofibril structure and exposing buried –SH groups, and this resultedin stronger inhibition of thermal aggregation therefore improved solubility of MP. More than 75% of heated MP remained soluble after the treatment with HPH and 160 μmol/g H 2 O 2 , while untreated samples formed a gel upon heating. These results proved that HPH combined with H 2 O 2 is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.",

keywords = "Heat stability, High-pressure homogenization, Hydrogen peroxide, Myofibrillar protein, Protein beverage, Sulfhydryl blockage",

author = "Xing Chen and Xiong, {Youling L.} and Xinglian Xu",

note = "Funding Information: This study was supported by the National Key R&D Program of China (No. 2018YFD0401203 ), the USDA National Institute of Food and Agriculture (Hatch Project 1005724), the National Natural Science Foundation of China (No. 31671875 ), an Oversea Study Fellowship from the China Scholarship Council (to Xing Chen), and the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD). Approved for publication as journal article no. 18-07-008 by the Director of the Kentucky Agricultural Experiment Station. Publisher Copyright: {\textcopyright} 2019 Elsevier Ltd",

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AU - Chen, Xing

AU - Xiong, Youling L.

AU - Xu, Xinglian

N1 - Funding Information: This study was supported by the National Key R&D Program of China (No. 2018YFD0401203 ), the USDA National Institute of Food and Agriculture (Hatch Project 1005724), the National Natural Science Foundation of China (No. 31671875 ), an Oversea Study Fellowship from the China Scholarship Council (to Xing Chen), and the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD). Approved for publication as journal article no. 18-07-008 by the Director of the Kentucky Agricultural Experiment Station. Publisher Copyright: © 2019 Elsevier Ltd

PY - 2019/7/1

Y1 - 2019/7/1

N2 - This study tested the potential of high-pressure homogenization (HPH, 69 MPa) combined with hydrogen peroxide (H 2 O 2 , at 0, 40, 80, 160 and 320 μmol/g protein) on enhancing the stability of myofibrillar protein (MP, 15 mg/mL) against thermal aggregation (95 °C for 10 min) in aqueous solution. The addition of H 2 O 2 blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of H 2 O 2 by disrupting the intact myofibril structure and exposing buried –SH groups, and this resultedin stronger inhibition of thermal aggregation therefore improved solubility of MP. More than 75% of heated MP remained soluble after the treatment with HPH and 160 μmol/g H 2 O 2 , while untreated samples formed a gel upon heating. These results proved that HPH combined with H 2 O 2 is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.

AB - This study tested the potential of high-pressure homogenization (HPH, 69 MPa) combined with hydrogen peroxide (H 2 O 2 , at 0, 40, 80, 160 and 320 μmol/g protein) on enhancing the stability of myofibrillar protein (MP, 15 mg/mL) against thermal aggregation (95 °C for 10 min) in aqueous solution. The addition of H 2 O 2 blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of H 2 O 2 by disrupting the intact myofibril structure and exposing buried –SH groups, and this resultedin stronger inhibition of thermal aggregation therefore improved solubility of MP. More than 75% of heated MP remained soluble after the treatment with HPH and 160 μmol/g H 2 O 2 , while untreated samples formed a gel upon heating. These results proved that HPH combined with H 2 O 2 is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.

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KW - Protein beverage

KW - Sulfhydryl blockage

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High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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