Effect of Transglutaminase on Reconstruction and Physicochemical Properties of Collagen Gel from Shark Type I Collagen
- 30 November 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Biomacromolecules
- Vol. 2 (1) , 105-110
- https://doi.org/10.1021/bm000085w
Abstract
The effects of microbial transglutaminase (MTGase) on type I collagen self-assembly and properties of reconstructed collagen fibrils from shark were investigated. Collagen self-assembly was accelerated with the addition of MTGase in dependence on that concentration. The relative amount of reconstructed collagen slightly decreased with MTGase. The diffusion coefficient of collagen gel was reduced by treatment with MTGase, and that suggested the reduction of mobility of the whole collagen network. At a high temperature, used to denature the collagen, MTGase-treated collagen gel remained as aggregates. By differential scanning calorimetry, the denaturation temperature of MTGase-treated collagen gel was about 2 °C higher than that of nontreated collagen gel. Treatment with MTGase yielded thermally stable cross-links in collagen molecules.Keywords
This publication has 6 references indexed in Scilit:
- Renaturation of α1 Chains from Shark Skin Collagen Type 1Journal of Food Science, 1995
- Strength of Protein Gels Prepared with Microbial Transglutaminase as Related to Reaction ConditionsJournal of Food Science, 1994
- Purification and Characterization of a Tissue-type Transglutaminase from Red Sea Bream (Pagrus major)Bioscience, Biotechnology, and Biochemistry, 1994
- Formation of ε‐(γ‐Glutamyl) Lysine Cross‐Link in Cured Horse Mackerel Meat Induced by DryingJournal of Food Science, 1993
- Investigation of viscosity and gelation properties of different mammalian and fish gelatinsFood Hydrocolloids, 1991
- Lower vertebrate collagen. Evidence for type I-like collagen in the skin of lamprey and sharkBiochimica et Biophysica Acta (BBA) - Protein Structure, 1981