Collagen production from chicken keel bone using acid and enzymatic treatment at a temperature of 30 °C

Abstract The aim of this study was to investigate the effect of acid pretreatment, temperature and enzyme concentration on the acid-enzymatic extraction of soluble collagen from chicken keel bone cartilage. A chemical composition analysis and protein profile characterization of this slaughter by-product were also conducted. The cartilages were extracted with 0.5 mol/L of acetic, lactic and citric acids for 24, 48 and 72 hours. Subsequently, optimization with a 22 factorial design was performed with three replications at the central point for a total of 7 experiments; the analyzed response was the collagen content of the obtained isolates. The cartilage under study has a high protein content (90.27% dry basis) consisting of approximately 35.7% collagen and is a source of essential and predominantly hydrophobic amino acids. Pretreatment with acetic acid for 24 hours led to greater extraction potential and consequently, a better collagen yield (30.12%). The electrophoretic profile of the obtained collagens revealed the existence of an α1 chain, indicating that this collagen was type II. Statistical analysis demonstrated that the acid-enzymatic procedure favored a temperature of 30 °C.

摘要 本研究旨在探究酸预处理、温度及酶浓度对酸酶法提取鸡胸龙骨软骨中可溶性胶原蛋白的影响，并对该屠宰副产物开展化学成分分析与蛋白质图谱表征。实验采用0.5 mol/L的乙酸、乳酸及柠檬酸分别对软骨进行24、48、72小时的提取处理；随后采用二因素二水平析因设计（2²析因设计）进行工艺优化，中心点设置3次重复，共计7组实验，以所得胶原分离物的胶原蛋白含量作为分析响应指标。
本研究对象软骨的蛋白质含量较高（以干重计为90.27%），其中胶原蛋白占比约35.7%，且富含必需氨基酸，氨基酸组成以疏水氨基酸为主。经24小时乙酸预处理的提取效果最优，胶原蛋白得率可达30.12%。所得胶原蛋白的电泳图谱显示存在α1肽链，表明该胶原蛋白为II型胶原。统计分析结果表明，该酸酶法提取工艺的适宜温度为30 ℃。