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Characterisation of hydrolysate for identifying initial peptide cleavage site of κ-casein by milk coagulating Wrightia tinctoria serine proteases
International Dairy Journal ( IF 3.1 ) Pub Date : 2020-11-27 , DOI: 10.1016/j.idairyj.2020.104934
Anusha Rajagopalan , Vasuki Aluru , Bindhu Omana Sukumaran

Research on identifying vegetable milk coagulants has gained momentum in the past few decades. Extent of casein hydrolysis and specific initial hydrolytic site on κ-casein are considered crucial in deciding suitability of plant proteases for cheese making. In the present study, three phase partitioned (TPP) proteases (serine) of Wrightia tinctoria stem were assayed to understand their specific cleavage site on κ-casein. Time dependent analysis of κ-casein hydrolysis by W. tinctoria proteases revealed 2 min incubation to be enough for hydrolysis to begin. Molecular mass of the resulting major peptide was confirmed to be 14,542.52 Da and was further characterised using LC/ESI-MSMS. The initial site of hydrolysis by W. tinctoria proteases on κ-casein was Asn123–Thr124, which is different from the expected Phe105–Met106 of rennin. The study concludes that even with its unique initial site of κ-casein hydrolysis, W. tinctoria proteases could influence milk clotting probably with distinct organoleptic properties.



中文翻译:

牛奶凝结Wrightia tinctoria丝氨酸蛋白酶的水解产物表征,以鉴定κ-酪蛋白的初始肽裂解位点

在过去的几十年中,鉴定植物乳凝结剂的研究获得了发展。酪蛋白水解的程度和κ-酪蛋白上的特定起始水解位点被认为是决定植物蛋白酶是否适合干酪生产的关键。在本研究中,测定了Wrightia tinctoria茎的三相分配(TPP)蛋白酶(丝氨酸),以了解其在κ-酪蛋白上的特异性切割位点。W. tinctoria蛋白酶对κ-酪蛋白水解的时间依赖性分析显示,孵育2分钟足以开始水解。确认得到的主要肽的分子量为14,542.52 Da,并使用LC / ESI-MSMS进一步表征。W. tinctoria蛋白酶在κ-酪蛋白上水解的起始位点是Asn123- Thr 124,与肾素的预期Phe 105- Met 106不同。研究得出的结论是,即使W. tinctoria蛋白酶具有独特的κ-酪蛋白水解起始位点,它也可能会影响牛奶凝结,具有明显的感官特性。

更新日期:2020-12-31
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