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Inicio  /  Coatings  /  Vol: 9 Par: 11 (2019)  /  Artículo
ARTÍCULO
TITULO

Effect of Transglutaminase Cross-Linking in Protein Isolates from a Mixture of Two Quinoa Varieties with Chitosan on the Physicochemical Properties of Edible Films

Monserrat Escamilla-García    
Luis Felipe Delgado-Sánchez    
Raquel Adriana Ríos-Romo    
Blanca E. García-Almendárez    
Georgina Calderón-Domínguez    
Juan Vicente Méndez-Méndez    
Aldo Amaro-Reyes    
Prospero Di Pierro and Carlos Regalado-González    

Resumen

The growing demand for minimally processed foods with a long shelf life and environmentally friendly materials has forced industry to develop new technologies for food preservation and handling. The use of edible films has emerged as an alternative solution to this problem, and mixtures of carbohydrates and proteins, may be formulated to improve their properties. The objective of this work was to evaluate the effect of protein cross-linking with transglutaminase (TG) of two varieties of quinoa protein isolate (Chenopodium quinoa) [Willd (QW), and Pasankalla (QP)] on the physicochemical and barrier properties of edible films based on chitosan (CT)-quinoa protein. The evaluated properties were water vapor permeability (WVP), solubility, adsorption, roughness determined by atomic force microscopy, and the interactions among the main film components determined by Raman spectroscopy. The results indicated that TG interacted with lysine of QW and QP. CT:QW (1:5, w/w) showed the lowest solubility (14.02 ± 2.17% w/w). WVP varied with the composition of the mixture. The WVP of CT:quinoa protein ranged from 2.85 to 9.95 × 10-11 g cm Pa-1 cm-2 s-1 without TG, whereas adding TG reduced this range to 2.42?4.69 × 10-11 g cm Pa-1 cm-2 s-1. The addition of TG to CT:QP (1:10, w/w) reduced the film surface roughness from 8.0 ± 0.5 nm to 4.4 ± 0.3 nm. According to the sorption isotherm, the addition of TG to CT-QW films improved their stability [monolayer (Xm) = 0.13 ± 0.02 %]. Films with a higher amount of cross-linking showed the highest improvement in the evaluated physical properties, but interactions among proteins that were catalyzed by TG depended on the protein source and profile.