Insight into the mechanism of myosin-fibrin gelation induced by non-disulfide covalent cross-linking. (June 2022)

• Record Type: Journal Article
• Authors: Du, Juanjuan; Cao, Jinxuan; Zhou, Changyu; Pan, Daodong; Geng, Fang; Wang, Ying
• Is Part Of: Food research international. Volume 156(2022)
• Publication Date: 2022-06
• Subjects: Myosin -- Fibrin -- ε-(γ-glutamyl)-lysine bonds -- Cross-linking sites -- LC-MS/MS; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2022.111168
• Languages: English
• ISSNs: 0963-9969

Abstract

Graphical abstract: Highlights: High level of ε-(γ-glutamyl)-lysine crosslinking enhanced the gel properties, rheological properties and WHC of myosin–fibrin gels. The crosslinking of myosin–fibrin accelerated the transformation of α-helix into β-sheet and formed a dense gel network with thick walls and low porosity. Myosin heavy chain was mainly involved in the cross-linking with α/β/γ-chains of fibrinogen. Lys 1085 of myosin heavy chain and Gln 195 of fibrinogen were mainly responsible for the formation of ε-(γ-glutamyl)-lysine bonds. Abstract: To explore the mechanism of non-disulfide covalent cross-linking between myosin and fibrin, the gel strength, texture parameters, rheological properties, protein conformation and microstructure and possible cross-linking sites were investigated during the gelling of myosin-fibrin gels. Higher ε-(γ-glutamyl)-lysine level in myosin-fibrin gels with transglutaminase significantly enhanced the textural properties, rheology properties and water holding capacity of myosin-fibrin gels, compared with pure myosin gel and myosin-fibrin gels with ehylenediaminetetraacetic acid; Fourier infrared spectra (FTIR) and circular dichroism (CD) spectra demonstrated that the structural transition from α-helix to β-sheet significantly was improved in myosin-fibrin gels with the addition of transglutaminase than other groups. Scanning electron microscopy revealed that high level of ε-(γ-glutamyl)-lysine cross-linking contributed to the formation of myosin-fibrin gels with a dense gel network structure with thick walls and low porosity. Myosin heavy chain was mainly involved in the cross-linking with α/β/γ-chains of fibrinogen; liquid chromatography-tandem mass spectrometry further demonstrated that Lys 1085 of myosin heavy chain was non-disulfide covalently bound to Gln 195 of fibrinogen to form "K-Q" isopeptide during the cross-linking of myosin-fibrin.