Synergistic recovery and enhancement of gelling properties of oxidatively damaged myofibrillar protein by l-lysine and transglutaminase

Yungang Cao; Baoling Li; Xin Fan; Jiankang Wang; Zhenbao Zhu; Junrong Huang; Youling L. Xiong

doi:10.1016/j.foodchem.2021.129860

Synergistic recovery and enhancement of gelling properties of oxidatively damaged myofibrillar protein by _l-lysine and transglutaminase

Yungang Cao, Baoling Li, Xin Fan, Jiankang Wang, Zhenbao Zhu, Junrong Huang, Youling L. Xiong

Animal and Food Sciences

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

63 Scopus citations

Abstract

The influence of combined Lysine (Lys) and transglutaminase (TG) on the conformation and gelling properties of oxidatively damaged myofibrillar protein (MP) was investigated. The addition of Lys (5 mM) significantly increased the α-helix content (by 47.8%) and decreased the particle size of oxidatively damaged MP, and improved the cooking yield (by 16.8%) and the breaking strength of MP gels (by 65.5%). The treatment with TG (E:S = 1:500) led to a slightly reduced α-helix content but improved breaking strength (by 41.8%) and cooking loss (by 13.3%) of the gels. Their combination (Lys + TG) showed the greatest and synergistic overall improvement, with the set gel displaying a fine, smooth and compact network structure. Notably, the gelling ability of oxidatively damaged MP upon Lys + TG treatment was significantly stronger than that of non-oxidized MP far exceeding its recovery. Therefore, significantly enhanced gelling properties of oxidatively damaged MP can be attained through the combination Lys and TG.

Original language	English
Article number	129860
Journal	Food Chemistry
Volume	358
DOIs	https://doi.org/10.1016/j.foodchem.2021.129860
State	Published - Oct 1 2021

Bibliographical note

Publisher Copyright:
© 2021

Funding

This research was supported by the National Natural Science Foundation of China (Grant No. 31801480 ), the Natural Science Basic Research Program of Shaanxi (2019JQ-397), and the Talent Development Fund of Shaanxi University of Science and Technology (No. 134080069).

Funders	Funder number
National Natural Science Foundation of China (NSFC)	31801480
National Natural Science Foundation of China (NSFC)
Shaanxi University of Science and Technology	134080069
Shaanxi University of Science and Technology
Natural Science Basic Research Program of Shaanxi Province	2019JQ-397
Natural Science Basic Research Program of Shaanxi Province

Keywords

-Lysine (PubChem CID5962)
Circular dichroism
Dithiothreitol (Compound CID446094)
Linoleic acid (PubChem CID5280450)
Microstructure
Particle size
Raman spectra
Rheology

ASJC Scopus subject areas

Analytical Chemistry
Food Science

Access to Document

10.1016/j.foodchem.2021.129860

Cite this

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title = "Synergistic recovery and enhancement of gelling properties of oxidatively damaged myofibrillar protein by l-lysine and transglutaminase",

abstract = "The influence of combined Lysine (Lys) and transglutaminase (TG) on the conformation and gelling properties of oxidatively damaged myofibrillar protein (MP) was investigated. The addition of Lys (5 mM) significantly increased the α-helix content (by 47.8\%) and decreased the particle size of oxidatively damaged MP, and improved the cooking yield (by 16.8\%) and the breaking strength of MP gels (by 65.5\%). The treatment with TG (E:S = 1:500) led to a slightly reduced α-helix content but improved breaking strength (by 41.8\%) and cooking loss (by 13.3\%) of the gels. Their combination (Lys + TG) showed the greatest and synergistic overall improvement, with the set gel displaying a fine, smooth and compact network structure. Notably, the gelling ability of oxidatively damaged MP upon Lys + TG treatment was significantly stronger than that of non-oxidized MP far exceeding its recovery. Therefore, significantly enhanced gelling properties of oxidatively damaged MP can be attained through the combination Lys and TG.",

keywords = "-Lysine (PubChem CID5962), Circular dichroism, Dithiothreitol (Compound CID446094), Linoleic acid (PubChem CID5280450), Microstructure, Particle size, Raman spectra, Rheology",

author = "Yungang Cao and Baoling Li and Xin Fan and Jiankang Wang and Zhenbao Zhu and Junrong Huang and Xiong, \{Youling L.\}",

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AU - Wang, Jiankang

AU - Zhu, Zhenbao

AU - Huang, Junrong

AU - Xiong, Youling L.

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N2 - The influence of combined Lysine (Lys) and transglutaminase (TG) on the conformation and gelling properties of oxidatively damaged myofibrillar protein (MP) was investigated. The addition of Lys (5 mM) significantly increased the α-helix content (by 47.8%) and decreased the particle size of oxidatively damaged MP, and improved the cooking yield (by 16.8%) and the breaking strength of MP gels (by 65.5%). The treatment with TG (E:S = 1:500) led to a slightly reduced α-helix content but improved breaking strength (by 41.8%) and cooking loss (by 13.3%) of the gels. Their combination (Lys + TG) showed the greatest and synergistic overall improvement, with the set gel displaying a fine, smooth and compact network structure. Notably, the gelling ability of oxidatively damaged MP upon Lys + TG treatment was significantly stronger than that of non-oxidized MP far exceeding its recovery. Therefore, significantly enhanced gelling properties of oxidatively damaged MP can be attained through the combination Lys and TG.

AB - The influence of combined Lysine (Lys) and transglutaminase (TG) on the conformation and gelling properties of oxidatively damaged myofibrillar protein (MP) was investigated. The addition of Lys (5 mM) significantly increased the α-helix content (by 47.8%) and decreased the particle size of oxidatively damaged MP, and improved the cooking yield (by 16.8%) and the breaking strength of MP gels (by 65.5%). The treatment with TG (E:S = 1:500) led to a slightly reduced α-helix content but improved breaking strength (by 41.8%) and cooking loss (by 13.3%) of the gels. Their combination (Lys + TG) showed the greatest and synergistic overall improvement, with the set gel displaying a fine, smooth and compact network structure. Notably, the gelling ability of oxidatively damaged MP upon Lys + TG treatment was significantly stronger than that of non-oxidized MP far exceeding its recovery. Therefore, significantly enhanced gelling properties of oxidatively damaged MP can be attained through the combination Lys and TG.

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