Controlled hydrolysis of cheese whey proteins using trypsin and α-chymotrypsin
Controlled hydrolysis of cheese whey proteins using trypsin and α-chymotrypsin
复制标题
DOI：
10.1385/abab:91-93:1-9:761
复制
发表时间：
2001-03-01
影响因子：
3
通讯作者：
Giordano, RDC
中科院分区：
文献类型：
--
作者：
Galvao, CMA;Silva, AFS;Giordano, RDC
本研究探讨了以干酪乳清蛋白为原料生产成分可控的蛋白质水解物。以乳清蛋白和纯化的β-乳球蛋白为底物，以胰酶和α-胰凝乳酶为催化剂，在两种温度和几种酶浓度下，对干酪乳清进行了表征和几种不同的酶浓度下的水解实验。将实验得到的最大水解度与理论值进行了比较，并计算了多肽组成。对于胰酶，产率达到100%；对于α-糜蛋白酶，其水解似乎依赖于寡肽的大小。结果表明，这两种酶对β-乳球蛋白有较强的水解性。胰酶和α-胰凝乳酶在40℃时比较稳定，但在55℃时酶活性急剧下降。
This study examined the production of protein hydrolysates with controlled composition from cheese whey proteins. Cheese whey was characterized and several hydrolysis experiments were made using whey proteins and purified beta -lactoglobulin, as substrates, and trypsin and a-chymotrypsin, as catalysts, at two temperatures and several enzyme concentrations. Maximum degrees of hydrolysis obtained experimentally were compared to the theoretical values and peptide compositions were calculated. For trypsin, 100% of yield was achieved; for alpha -chymotrypsin, hydrolysis seemed to be dependent on the oligopeptide size. The results showed that the two proteases could hydrolyze beta -lactoglobulin. Trypsin and alpha -chymotrypsin were stable at 40 degreesC, but a sharp decrease in the protease activity was observed at 55 degreesC.