A partially puriüed globulin from cowpea seeds was polymerised by calcium-independent microbial transglutaminase. The level of free amino groups in the globulin decreased with increase in enzyme concentration, suggesting that the cross-linking reaction involved participation of the amino residues. A
Effect of microbial transglutaminase on the functional properties of megrim (Lepidorhombus boscii) skin gelatin
✍ Scribed by M Carmen Gómez-Guillén; Ana Isabel Sarabia; M Teresa Solas; Pilar Montero
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 338 KB
- Volume
- 81
- Category
- Article
- ISSN
- 0022-5142
- DOI
- 10.1002/jsfa.865
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✦ Synopsis
Abstract
This paper examines the effect of a microbial transglutaminase (TGase) on the gelling and viscoelastic properties of a gelatin from megrim (Lepidorhombus boscii) skins. Although TGase extended the setting time of fish gelatin, it was found that melting temperature, gel strength and viscosity in solution at 60 °C were considerably increased by the covalent cross‐linking action of the enzyme, as observed by SDS‐PAGE and SEM. Increasing concentrations of TGase increased the elasticity and cohesiveness of gelatin gels but reduced gel strength and hardness. Partial inactivation of the enzyme was achieved thermally without negatively affecting the properties of the gelatin; whether or not gelatin is thermoreversible depends essentially on the degree of enzyme inactivation.
© 2001 Society of Chemical Industry
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