Schlegel Katharina, Sontheimer Katharina, Eisner Peter, Schweiggert-Weisz Ute
Emil Fischer Center Department of Chemistry and Pharmacy Friedrich-Alexander-Universität Erlangen-Nürnberg Erlangen Germany.
Department Food Process Development Fraunhofer Institute for Process Engineering and Packaging IVV Freising Germany.
Food Sci Nutr. 2019 Dec 1;8(7):3041-3051. doi: 10.1002/fsn3.1286. eCollection 2020 Jul.
The modification of lupin protein isolates (LPI) by means of enzymatic hydrolysis ( cultivar Boregine) was performed with four enzyme preparations (Alcalase 2.4 L, Papain, Corolase 7089, and Neutrase 0.8 L) in a one- and two-step process to determine the efficacy for the destruction of major IgE-reactive polypeptides and the evaluation of the technofunctional and sensory properties of lupin protein hydrolysates. Combinations of Alcalase 2.4 L and Papain were most effective in the degradation of polypeptides in as measured by sodium dodecylsulfate-polyacrylamide gel electrophoresis. The enzymatic hydrolysis of the LPI increased their technofunctional properties such as protein solubility, foam activity, and emulsifying capacity almost independently of the enzyme preparation used. The sensory results showed a significant increase in bitterness from 1.9 for LPI to 5.7 for the combination of Alcalase 2.4 L and Papain in one-step process. The aroma attributes of the hydrolysates were very similar to untreated LPI. The results of this study show the possibility of enzymatic hydrolysis of LPI to destroy the major IgE-reactive polypeptides that increase the technofunctional properties of the isolates and thus their use in human nutrition as food ingredients.
采用四种酶制剂（碱性蛋白酶2.4L、木瓜蛋白酶、嗜热菌蛋白酶7089和中性蛋白酶0.8L），通过一步法和两步法对羽扇豆分离蛋白（LPI，品种为Boregine）进行酶解修饰，以确定破坏主要IgE反应性多肽的效果，并评估羽扇豆蛋白水解物的技术功能和感官特性。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定，碱性蛋白酶2.4L和木瓜蛋白酶的组合在降解多肽方面最有效。LPI的酶解几乎与所用酶制剂无关，提高了其技术功能特性，如蛋白质溶解度、泡沫活性和乳化能力。感官结果显示，在一步法中，苦味从LPI的1.9显著增加到碱性蛋白酶2.4L和木瓜蛋白酶组合的5.7。水解物的香气特性与未处理的LPI非常相似。本研究结果表明，LPI酶解有可能破坏主要的IgE反应性多肽，这些多肽可提高分离蛋白的技术功能特性，从而使其作为食品成分用于人类营养。
