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Maillard reaction can influence the functionalities of myofibrillar protein (MP). Protein-saccharide Maillard-type conjugates improve the solubility of MP but impair its thermal gelling ability. Besides, the influences of Maillard reaction occurred between reducing sugar and free amino acids on MP were not inspected yet. In this study, arginine-glucose Maillard reaction products (MRPs) were adopted to investigate their effects on the physicochemical and gel properties of chicken MP. The results showed that Arg-Glc MRPs significantly decreased surface hydrophobicity and the content of reactive sulfhydryl group, subsequently influenced the gelling behavior and gel properties, e.g., water holding capacity and gel strength. The dynamic rheological results revealed that MRPs reduced the storage modulus value effectively. Scanning electron microscopy showed that the three-dimensional network structure of MP gel became coarser and irregular by the treatment of Arg-Glc MRPs. These results suggested that Arg-Glc MRPs have influences on both the physicochemical properties and the gel properties of MP, which may provide new information to the effects of MRPs on the water holding capacity and texture of meat products. • MRPs lowered the gel strength and the G′ values of myofibrillar protein (MP). • Arg-Glc MRPs also reduced the surface hydrophobicity and reactive SH group content. • MP gels displayed a coarser and more irregular network by treating with the MRPs. [ABSTRACT FROM AUTHOR]

A simple, efficient, and low-cost Maillard reaction method was developed through ethanol-water pretreatment. The formation of whey protein isolate (WPI)–dextran conjugates was confirmed using the degree of glycosylation, ultraviolet absorbance, browning intensity, color, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The significant conformational changes were illuminated because of the higher wavenumber shift of absorption peaks of FTIR amide I, II, and III bands, the reduction of fluorescent signal, and the decrease of surface hydrophobicity. Scanning electron microscopy revealed the morphological transition of WPI from a smooth sphere to an inhomogeneous block structure with rough and uneven surface before and after covalent grafting of dextran. The strong steric hindrance and abundant hydrophilic hydroxyl groups from covalently conjugated dextran dramatically inhibited the aggregation between conjugate molecules which exhibited low turbidity and good solubility in a wide pH range from 2.0 to 10.0. Emulsifying activity and emulsifying stability of WPI were significantly improved after glycosylation. This work will be beneficial to control the formation of light-colored Maillard reaction products under high substrate concentration, high reaction rate, and low water content at mild temperatures for short processing time, and to facilitate the large-scale preparation of glycosylated protein with desirable physicochemical properties. [Display omitted] • A simple, efficient, and low-cost Maillard reaction method was developed. • Maillard reaction time was largely shorten through ethanol-water pretreatment. • Light-colored Maillard reaction products were obtained at mild temperatures. • Advantages were high concentration, high rate, and limited waste water discharge. [ABSTRACT FROM AUTHOR]