Abstract
Transglutaminase (TGase) was cross-linked with glutaraldehyde, and cross-linked crystalline transglutaminase was immobilized on a polypropylene microporous membrane by UV-induced grafting. Immobilized enzyme activity were calculated to be 0.128 U/cm2 polypropylene microporous membrane. The microstructure and enzyme characteristics of free, cross-linked and immobilized transglutaminase were compared. The optimum temperature of free transglutaminase was determined to be approximately 40 °C, while cross-linking and immobilization resulted in an increase to approximately 45 °C and 50 °C. At 60 °C, immobilized, cross-linked and free transglutaminase retained 91.7 ± 1.20%, 63.2 ± 1.05% and 37.9 ± 0.98% maximum activity, respectively. The optimum pH was unaffected by the state of transglutaminase. However, the thermal and pH stabilities of cross-linked and immobilized transglutaminase were shown to increase.
Highlights
Transglutaminase (TGase; protein-glutamine-glutamyltransferase, EC 2.3.2.13). catalyzes the acyl-transfer reaction in which the γ-carboxyamide groups of glutamine residues in proteins, peptides and various primary amines, act as acyl donors and primary amino groups including ε-amino groups of lysine residues, either as peptide-proteins bound or free lysine, act as the acyl acceptors [1,2,3,4,5]
Units of enzyme activity immobilized on spacers were calculated to be 0.128 U/cm2 polypropylene microporous membrane
Surface characteristics and cross-sectional morphology of free, cross-linked and immobilized transglutaminase and polypropylene microporous membranes were analyzed by Scanning electron microscopy (SEM) (Figure 1)
Summary
Transglutaminase (TGase; protein-glutamine-glutamyltransferase, EC 2.3.2.13). catalyzes the acyl-transfer reaction in which the γ-carboxyamide groups of glutamine residues in proteins, peptides and various primary amines, act as acyl donors and primary amino groups including ε-amino groups of lysine residues, either as peptide-proteins bound or free lysine, act as the acyl acceptors [1,2,3,4,5]. Catalyzes the acyl-transfer reaction in which the γ-carboxyamide groups of glutamine residues in proteins, peptides and various primary amines, act as acyl donors and primary amino groups including ε-amino groups of lysine residues, either as peptide-proteins bound or free lysine, act as the acyl acceptors [1,2,3,4,5] These reactions are dependent on a number of factors, including pH and temperature. In the meat industry, using transglutaminase to cross-link proteins has been found feasible. The TGase enzyme catalyzes cross-linking between protein molecules [21]. Transglutaminase was cross-linked and immobilized on a polypropylene microporous membrane to improve the enzyme characteristics. Scanning electron microscopy (SEM) was used to study the microstructure of the free, cross-linked and immobilized crystalline transglutaminase. The optimal temperature and pH conditions for transglutaminase activity were determined in addition to analysis of thermal and pH stabilities
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