Enzymatically deamidated pork myofibrillar protein can form thermo-reversible gels

By using protein-glutaminase (PG) deamidation, thermo-reversible gel of pork myofibrillar protein (PMP) can be prepared. This study aims to reveal the connection between PMP thermo-reversible gel and the coiled-coil. The research explores how the water-holding capacity and reversibility of these gels improve with increased deamidation time. At a deamidation duration of 4 h, the gel strength reaches its peak. Moreover, PG deamidation significantly enhances the α-helix content to over 60 %. This change boosts the likelihood of α-helix interactions while increasing coiled helix content. Notably, the interference experiment of trifluoroethanol suggests that a high concentration of coiled coils is essential for imparting reversible properties to the deamidated myofibrillar protein gel. This research contributes to the advancement of protein micro-modification in the custom manufacturing of muscle protein-based soft meal products.

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Publication Details

Journal
International Journal of Biological Macromolecules
Published
2024-12-20
DOI
https://doi.org/10.1016/j.ijbiomac.2024.139039
Citations
1
Primary Topic
Muscle metabolism and nutrition
Type
article
Field-Weighted Citation Impact
0.33
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article

Enzymatically deamidated pork myofibrillar protein can form thermo-reversible gels

Jianlian Huang, Xidong Jiao, Bowen Yan, Daming Fan et al.
1 citations
International Journal of Biological Macromolecules
Muscle metabolism and nutrition
0.33
article

Enzymatically deamidated pork myofibrillar protein can form thermo-reversible gels

Jianlian Huang, Xidong Jiao, Bowen Yan, Daming Fan, Xing Chen, Hao Zhang, Tao Yuan, Yanyun Zhang, Xingwei Li, Nana Zhang
article en
1 citations

Abstract

By using protein-glutaminase (PG) deamidation, thermo-reversible gel of pork myofibrillar protein (PMP) can be prepared. This study aims to reveal the connection between PMP thermo-reversible gel and the coiled-coil. The research explores how the water-holding capacity and reversibility of these gels improve with increased deamidation time. At a deamidation duration of 4 h, the gel strength reaches its peak. Moreover, PG deamidation significantly enhances the α-helix content to over 60 %. This change boosts the likelihood of α-helix interactions while increasing coiled helix content. Notably, the interference experiment of trifluoroethanol suggests that a high concentration of coiled coils is essential for imparting reversible properties to the deamidated myofibrillar protein gel. This research contributes to the advancement of protein micro-modification in the custom manufacturing of muscle protein-based soft meal products.

International Journal of Biological MacromoleculesVol. 290
Jiangnan University (CN), WuXi AppTec (China) (CN), Institute of Refrigeration (GB), State Key Laboratory of Food Science and Technology (CN)
Openalex Percentile: Top 38%
Muscle metabolism and nutrition
0.33
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Enzymatically deamidated pork myofibrillar protein can form thermo-reversible gels — Jianlian Huang, Xidong Jiao, et al. · International Journal of Biological Macromolecules (2024) | TGRS Research Map | TGRS