Universidade Federal do Ceará, Departamento de Bioquímica e Biologia Molecular, Fortaleza, Ceará CEP 60.440-970, Brazil.
Instituto de Estudios Inmunológicos y Fisiopatológicos IIFP (CONICET and University of La Plata). La Plata, Argentina.
Food Chem. 2019 Jun 30;284:245-253. doi: 10.1016/j.foodchem.2019.01.123. Epub 2019 Jan 25.
The present study evaluated four laticifer fluids as a novel source of peptidases capable of hydrolyzing proteins in cow's milk. The latex peptidases from Calotropis procera (CpLP), Cryptostegia grandiflora (CgLP), and Carica papaya (CapLP) were able to perform total hydrolysis of caseins after 30 min at pH 6.5, as confirmed by a significant reduction in the residual antigenicity. Casein hydrolysis by Plumeria rubra latex peptidases (PrLP) was negligible. Moreover, whey proteins were more resistant to proteolysis by latex peptidases; however, heat pretreatment of the whey proteins enhanced the degree of hydrolysis and reduced the residual antigenicity of the hydrolysates. The in vivo assays show that the cow's milk proteins hydrolysed by CgLP and CapLP exhibited no immune reactions in mice allergic to cow's milk, similar to a commercial partially hydrolysed formula. Thus, these peptidases are promising enzymes for the development of novel hypoallergenic formulas for children with a milk allergy.
本研究评估了四种乳管液作为一种新型的蛋白水解酶来源，能够水解牛奶中的蛋白质。来自 Calotropis procera（CpLP）、Cryptostegia grandiflora（CgLP）和 Carica papaya（CapLP）的乳管液蛋白酶在 pH 值为 6.5 下 30 分钟内即可完成酪蛋白的完全水解，这一点得到了确认，因为残余抗原性显著降低。Plumeria rubra 乳管液蛋白酶（PrLP）对酪蛋白的水解作用可以忽略不计。此外，乳清蛋白对乳管液蛋白酶的水解具有更强的抵抗力；然而，乳清蛋白的热预处理增强了水解程度，并降低了水解产物的残余抗原性。体内试验表明，对牛奶过敏的小鼠对 CgLP 和 CapLP 水解的牛奶蛋白没有免疫反应，类似于商业部分水解配方。因此，这些蛋白酶是开发针对牛奶过敏儿童的新型低致敏配方的有前途的酶。
