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Algerian cardoon flowers express a large spectrum of coagulant enzymes with potential applications in cheesemaking
International Dairy Journal ( IF 3.1 ) Pub Date : 2020-06-01 , DOI: 10.1016/j.idairyj.2020.104689
Abdellah Zikiou , Ana Cristina Esteves , Eduardo Esteves , Nuno Rosa , Sandra Gomes , António Pedro Louro Martins , Mohammed Nasreddine Zidoune , Marlene Barros

Abstract Proteases from flowers of Algerian cultivated and wild cardoons were purified, characterised and compared with those purified from flowers of a Portuguese variety. Three cardosins (A0, A and B) were obtained from each variety. All of them were dimeric and comprised heavy and light chain. Cardosins from Algerian varieties presented higher molecular masses and were less glycosylated than their Portuguese counterparts. Milk coagulation and curd yield parameters revealed a large difference between cardosins A0, A and B and among the same cardosin from different origins. The enzymatic specificity of cardosins, studied against β-chain of oxidised insulin and κ-casein, showed no prevalent effect of varieties. However, compared with cardosins A0 and A, cardosin B was more proteolytic and led to more complex digestion profiles. The present study reports the first description of the diversity of cardosins in Algerian cardoon flowers and sustains their potential use as milk coagulants for cheesemaking.

中文翻译:

阿尔及利亚刺猬花表达了大范围的凝固酶,在奶酪制作中具有潜在应用

摘要 对来自阿尔及利亚栽培和野生刺猬花的蛋白酶进行纯化、表征并与从葡萄牙品种花中纯化的蛋白酶进行比较。从每个品种中获得了三种卡多辛(A0、A 和 B)。它们都是二聚体并包含重链和轻链。与葡萄牙品种相比,来自阿尔及利亚品种的卡多辛分子质量更高,糖基化程度更低。牛奶凝固和凝乳产量参数显示卡多素 A0、A 和 B 之间以及来自不同来源的相同卡多素之间存在很大差异。针对氧化胰岛素和κ-酪蛋白的β-链研究的cardosin 的酶特异性表明品种没有普遍影响。然而,与cardosin A0 和A 相比,cardosin B 具有更强的蛋白水解能力,并导致更复杂的消化谱。
更新日期:2020-06-01
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