Characterization of hydrolysates of collagen from mechanically separated chicken meat residue

Abstract Obtaining collagen and hydrolysates from mechanically separated chicken meat residue is an excellent way to add value to this waste. The aims of this study were to obtain collagen hydrolysates from chicken MSM residue using Alcalase® and Flavourzyme® enzymes, as well characterizing the functional, structural and thermal stability properties. The highest degree of hydrolysis was obtained using Alcalase®, 36.11%, while using Flavourzyme® resulted in 12.02%. The DSC analysis of the collagen indicated a denaturation temperature of 46.47 °C. The FTIR spectra of the crude collagen showed absorption peaks that were characteristic of amide bands A, B, I, II and III. In the spectra of the hydrolysed the area of the amide bands was reduced, and some peaks appeared between 800 and 1,200 cm-1. The disappearance of high molecular weight bands in the SDS-PAGE analysis also confirmed the hydrolysis of collagen. After the hydrolysis, the collagen presented reduced viscosity, the capacity to form foam, and foam stability. The emulsifying activity index was high in the hydrolysates in relation to the crude collagen. Thus, the use of Alcalase® and Flavourzyme® to obtain hydrolysates from collagen derived from chicken MSM residue was shown to be viable, and potentially useful for industrial applications.摘要：从机械分离鸡肉残渣中提取胶原蛋白及其水解物，是提升该类废弃物附加值的优良途径。本研究旨在利用碱性蛋白酶（Alcalase®）和风味蛋白酶（Flavourzyme®）从鸡机械分离肉（Mechanical Separated Meat, MSM）残渣中制备胶原蛋白水解物，并对其功能特性、结构特性及热稳定性能进行表征。采用Alcalase®水解时，水解度最高，达36.11%；而使用Flavourzyme®时水解度为12.02%。对胶原蛋白的差示扫描量热法（DSC）分析显示，其变性温度为46.47℃。粗制胶原蛋白的傅里叶变换红外光谱（FTIR）显示出酰胺A、B、I、II及Ⅲ带的特征吸收峰；水解产物的光谱中，酰胺带的面积有所减小，且在800~1200 cm⁻¹区间出现了部分新峰。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）分析中，高分子量条带的消失也证实了胶原蛋白的水解过程。水解处理后，产物的黏度、泡沫生成能力及泡沫稳定性均有所降低；相较于粗制胶原蛋白，水解物的乳化活性指数更高。综上，利用Alcalase®和Flavourzyme®从鸡MSM残渣来源的胶原蛋白中制备水解物的方案具有可行性，在工业应用中具备潜在应用价值。