Caseinate–gelatin and caseinate‐hydrolyzed gelatin composites formed via transglutaminase: chemical and functional properties

Abstract

The composites generated were different in chemical characteristics and better in viscosity and emulsion stability than original caseinate. They might have potential as protein thickeners and emulsifiers. CLSM is a better technique to assess emulsion stability of food proteins than the classic turbidity method.

Properties of bovine gelatin cross-linked by a mixture of two oxidases (horseradish peroxidase and glucose oxidase) and glucose

“…Gelatin films cross-linked by glutaraldehyde (Bigi, Cojazzi, Panzavolta, Rubini, & Roveri, 2001) and dialdehyde alginate (Boanini, Rubini, Panzavolta, & Bigi, 2010) were reported to have increased thermal stability at higher denaturation temperatures (up to 30°C for glutaraldehyde, and 3°C for dialdehyde alginate). TGase-induced cross-linking was reported to enhance the thermal stability of caseinate (Luo & Zhao, 2014) and β-lactoglobulin in heat-shocked whey proteins (Damodaran & Agyare, 2013). The present study shares the same conclusions as these studies: cross-linked gelatin showed higher resistance to thermal treatment due to dityrosine formation in its molecules.…”

“…Thermogravimetric (TG) analysis of the samples was carried out using a TG analyser (SDT Q600, TA Instruments Inc., New Castle, DE, USA) as previously reported (Luo & Zhao, 2014), with slight modification. Dried samples were maintained in a desiccator at room temperature with saturated NaCl solution (relative humidity~75.5%) for 72 h, to ensure that the samples adsorbed water completely.…”

Pre‐deamidation of soy protein isolate exerts impacts on transglutaminase‐induced glucosamine glycation and cross‐linking as well as properties of the products

“…Thermogravimetry analysis is a useful tool to describe thermal behaviour and stability of synthetic polymers, organic materials and biopolymers during heating . TG and DTG were also used in a previous study to show successfully that conjugation of the plastic gelatin products into casein by TGase brought about lower thermal stability . It was found that deamidation decreased thermal stability of betaB1‐crystallin, supporting that GC‐DSPI1 and GC‐DSPI2 (as two deamidated protein products) were less stable than GC‐SPI.…”

Gelation kinetics and characterization of enzymatically enhanced fish scale gelatin–pectin coacervate

“…The transparency of treated FSG-HMP solution was determined by the measurement of turbidity using a UV-visible spectrophotometer (Evolution Array, Thermo-Scientific, Waltham, MA, USA) at a wavelength of 600 nm according to the method of Luo et al 21 Double-distilled water was used as the blank reference. Each turbidity measurement was carried out in triplicate and calculated as follows:…”