Role of disulphide linkages between protein-coated lipid droplets and the protein matrix in the rheological properties of porcine myofibrillar protein-peanut oil emulsion composite gels

Mangang Wu; Youling L. Xiong; Jie Chen

doi:10.1016/j.meatsci.2011.01.014

Role of disulphide linkages between protein-coated lipid droplets and the protein matrix in the rheological properties of porcine myofibrillar protein-peanut oil emulsion composite gels

Mangang Wu, Youling L. Xiong, Jie Chen

Animal and Food Sciences

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

97 Scopus citations

Abstract

The objective of the study was to establish disulphide interaction between protein-coated oil droplets and the surrounding protein matrix in myofibrillar protein (MP)-emulsion composite gels. An MP-stabilized peanut oil emulsion was treated with 0, 1, 3, 5 and 10. mM N-ethylmaleimide (NEM, a sulphydryl-blocking agent) and subsequently incorporated into a bulk MP sol to produce 5%-lipid, 2%-protein composites at pH 6.2. About 69% of sulphydryls in the emulsion (1% protein) were blocked by 1. mM NEM, and almost all were bound at ≥ 3. mM NEM. The loss of free sulphydryls resulted in a significant drop in the storage modulus (G') and rupture force of the composite gels. Microstructural examination revealed pores and oil leakage from emulsion droplets by NEM treatments, corresponding to declining rheological properties of the MP-emulsion composites. The results supported the hypothesis that disulphide cross-linking between MP-coated oil droplets and protein matrix contributed to the stabilization and reinforcement of protein-emulsion composite gels formed in comminuted muscle foods.

Original language	English
Pages (from-to)	384-390
Number of pages	7
Journal	Meat Science
Volume	88
Issue number	3
DOIs	https://doi.org/10.1016/j.meatsci.2011.01.014
State	Published - Jul 2011

Bibliographical note

Funding Information:
The study was supported by the National Natural Science Foundation of China (grant no. 30972290 ), Program for Changjiang Scholars and Innovative Research Team, China (grant nos. IRT0627 and NCET-07-0377 ), the Ministry of Science and Technology, China (Grant no. 2010CB535014 ), and the State Key Laboratory of Food Science and Technology, Jiangnan University (grant no. SKLF-MB-200803 ).

Funding

The study was supported by the National Natural Science Foundation of China (grant no. 30972290 ), Program for Changjiang Scholars and Innovative Research Team, China (grant nos. IRT0627 and NCET-07-0377 ), the Ministry of Science and Technology, China (Grant no. 2010CB535014 ), and the State Key Laboratory of Food Science and Technology, Jiangnan University (grant no. SKLF-MB-200803 ).

Funders	Funder number
Program for Changjiang Scholars and Innovative Research Team, China	NCET-07-0377, IRT0627
National Natural Science Foundation of China (NSFC)	30972290
Ministry of Science and Technology of the People's Republic of China	2010CB535014
Jiangnan University	SKLF-MB-200803
State Key Laboratory of Food Science and Technology

Keywords

Disulphide
Emulsion
Gelation
Myofibrillar protein
N-ethylmaleimide

ASJC Scopus subject areas

Food Science

Access to Document

10.1016/j.meatsci.2011.01.014

Cite this

@article{bb19627e72c74f33a06d439475b048c4,

title = "Role of disulphide linkages between protein-coated lipid droplets and the protein matrix in the rheological properties of porcine myofibrillar protein-peanut oil emulsion composite gels",

abstract = "The objective of the study was to establish disulphide interaction between protein-coated oil droplets and the surrounding protein matrix in myofibrillar protein (MP)-emulsion composite gels. An MP-stabilized peanut oil emulsion was treated with 0, 1, 3, 5 and 10. mM N-ethylmaleimide (NEM, a sulphydryl-blocking agent) and subsequently incorporated into a bulk MP sol to produce 5%-lipid, 2%-protein composites at pH 6.2. About 69% of sulphydryls in the emulsion (1% protein) were blocked by 1. mM NEM, and almost all were bound at ≥ 3. mM NEM. The loss of free sulphydryls resulted in a significant drop in the storage modulus (G') and rupture force of the composite gels. Microstructural examination revealed pores and oil leakage from emulsion droplets by NEM treatments, corresponding to declining rheological properties of the MP-emulsion composites. The results supported the hypothesis that disulphide cross-linking between MP-coated oil droplets and protein matrix contributed to the stabilization and reinforcement of protein-emulsion composite gels formed in comminuted muscle foods.",

keywords = "Disulphide, Emulsion, Gelation, Myofibrillar protein, N-ethylmaleimide",

author = "Mangang Wu and Xiong, {Youling L.} and Jie Chen",

note = "Funding Information: The study was supported by the National Natural Science Foundation of China (grant no. 30972290 ), Program for Changjiang Scholars and Innovative Research Team, China (grant nos. IRT0627 and NCET-07-0377 ), the Ministry of Science and Technology, China (Grant no. 2010CB535014 ), and the State Key Laboratory of Food Science and Technology, Jiangnan University (grant no. SKLF-MB-200803 ).",

year = "2011",

month = jul,

doi = "10.1016/j.meatsci.2011.01.014",

language = "English",

volume = "88",

pages = "384--390",

number = "3",

}

TY - JOUR

T1 - Role of disulphide linkages between protein-coated lipid droplets and the protein matrix in the rheological properties of porcine myofibrillar protein-peanut oil emulsion composite gels

AU - Wu, Mangang

AU - Xiong, Youling L.

AU - Chen, Jie

N1 - Funding Information: The study was supported by the National Natural Science Foundation of China (grant no. 30972290 ), Program for Changjiang Scholars and Innovative Research Team, China (grant nos. IRT0627 and NCET-07-0377 ), the Ministry of Science and Technology, China (Grant no. 2010CB535014 ), and the State Key Laboratory of Food Science and Technology, Jiangnan University (grant no. SKLF-MB-200803 ).

PY - 2011/7

Y1 - 2011/7

N2 - The objective of the study was to establish disulphide interaction between protein-coated oil droplets and the surrounding protein matrix in myofibrillar protein (MP)-emulsion composite gels. An MP-stabilized peanut oil emulsion was treated with 0, 1, 3, 5 and 10. mM N-ethylmaleimide (NEM, a sulphydryl-blocking agent) and subsequently incorporated into a bulk MP sol to produce 5%-lipid, 2%-protein composites at pH 6.2. About 69% of sulphydryls in the emulsion (1% protein) were blocked by 1. mM NEM, and almost all were bound at ≥ 3. mM NEM. The loss of free sulphydryls resulted in a significant drop in the storage modulus (G') and rupture force of the composite gels. Microstructural examination revealed pores and oil leakage from emulsion droplets by NEM treatments, corresponding to declining rheological properties of the MP-emulsion composites. The results supported the hypothesis that disulphide cross-linking between MP-coated oil droplets and protein matrix contributed to the stabilization and reinforcement of protein-emulsion composite gels formed in comminuted muscle foods.

AB - The objective of the study was to establish disulphide interaction between protein-coated oil droplets and the surrounding protein matrix in myofibrillar protein (MP)-emulsion composite gels. An MP-stabilized peanut oil emulsion was treated with 0, 1, 3, 5 and 10. mM N-ethylmaleimide (NEM, a sulphydryl-blocking agent) and subsequently incorporated into a bulk MP sol to produce 5%-lipid, 2%-protein composites at pH 6.2. About 69% of sulphydryls in the emulsion (1% protein) were blocked by 1. mM NEM, and almost all were bound at ≥ 3. mM NEM. The loss of free sulphydryls resulted in a significant drop in the storage modulus (G') and rupture force of the composite gels. Microstructural examination revealed pores and oil leakage from emulsion droplets by NEM treatments, corresponding to declining rheological properties of the MP-emulsion composites. The results supported the hypothesis that disulphide cross-linking between MP-coated oil droplets and protein matrix contributed to the stabilization and reinforcement of protein-emulsion composite gels formed in comminuted muscle foods.

KW - Disulphide

KW - Emulsion

KW - Gelation

KW - Myofibrillar protein

KW - N-ethylmaleimide

UR - http://www.scopus.com/inward/record.url?scp=79952814081&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79952814081&partnerID=8YFLogxK

U2 - 10.1016/j.meatsci.2011.01.014

DO - 10.1016/j.meatsci.2011.01.014

M3 - Article

C2 - 21342749

AN - SCOPUS:79952814081

SN - 0309-1740

VL - 88

SP - 384

EP - 390

JO - Meat Science

JF - Meat Science

IS - 3

ER -

Role of disulphide linkages between protein-coated lipid droplets and the protein matrix in the rheological properties of porcine myofibrillar protein-peanut oil emulsion composite gels

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this