Transglutaminase Crosslinked Gelatin Films Extracted from Tanned Leather Waste

Abstract

The production of biodegradable polymers has proved to be a promising alternative, since these materials have accelerated degradation, contributing to the reduction of residues and the reduction of environmental pollution. The tannery wastes contain considerable collagen and can be used for gelatin extraction and film production for use in agriculture. Gelatin-based films, however, present some challenges for practical application, such as permeability and solubility in water, parameters that can be improved through the crosslinking process by employing enzymes, promoting the union of polymeric gelatin chains. In this context, the action of the enzyme transglutaminase was investigated to improve the properties of gelatin films recovered from leather and chitosan residues, which were evaluated according to thickness, solubility, permeability, mechanical properties, and soil degradation. The results indicated that the enzyme concentration in the films had a significant effect on the properties of water permeability and solubility and strain to rupture. The evaluation of soil degradation showed that films with higher enzyme addition took longer to be degraded.

The coexistence of carboxymethylcellulose and transglutaminase modified the physicochemical properties and structure of whey protein concentrate films

“…Baggio et al . (2021) reported the mechanical properties of TG cross‐linked deamidated gluten films were investigated and it was found that TS and EAB of gluten films increased in combination with TG, explaining that the rigidity of the covalent bonds formed by TG cross‐linked gluten was sufficient to increase the fracture elongation of the film. In general, the addition of CMC effectively improved the mechanical properties of WPC single film.…”

“…This is similar to previous research by Pratiwi and Setiadi (2021), who found that TG could improve mechanical properties of gelatin by inducing cross-linking of peptides with polypeptidebound glutamine residues and various primary amines to promote substantial intramolecular polymerisation of peptides in gelatin. Baggio et al (2021) reported the mechanical properties of TG cross-linked deamidated gluten films were investigated and it was found that TS and EAB of gluten films increased in combination with TG, explaining that the rigidity of the covalent bonds formed by TG cross-linked gluten was sufficient to increase the fracture elongation of the film. In general, the addition of CMC effectively improved the mechanical properties of WPC single film.…”