Process Engineering Laboratory, State University of Southwest Bahia, BR 415, km 04, s/n, Itapetinga, Bahia 45700-000, Brazil.
Process Engineering Laboratory, State University of Southwest Bahia, BR 415, km 04, s/n, Itapetinga, Bahia 45700-000, Brazil.
Food Res Int. 2024 Jun;186:114161. doi: 10.1016/j.foodres.2024.114161. Epub 2024 Feb 28.
In this article, the synthesis of antioxidant peptides in the enzymatic hydrolysis of caprine casein was analyzed at three different time points (60 min, 90 min, and 120 min) using immobilized pepsin on activated and modified carbon (AC, ACF, ACG 50, ACG 100). The immobilization assays revealed a reduction in the biocatalysts' activity compared to the free enzyme. Among the modified ones, ACG 50 exhibited greater activity and better efficiency for reuse cycles, with superior values after 60 min and 90 min. Peptide synthesis was observed under all studied conditions. Analyses (DPPH, β-carotene/linoleic acid, FRAP) confirmed the antioxidant potential of the peptides generated by the immobilized enzyme. However, the immobilized enzyme in ACG 50 and ACG 100, combined with longer hydrolysis times, allowed the formation of peptides with an antioxidant capacity greater than or equivalent to those generated by the free enzyme, despite reduced enzymatic activity.
本文分析了在三种不同时间点（60min、90min 和 120min）下，使用固定化胃蛋白酶在活化和改性碳（AC、ACF、ACG50、ACG100）上对山羊乳清蛋白进行酶解时抗氧化肽的合成。固定化实验表明，与游离酶相比，生物催化剂的活性降低。在改性酶中，ACG50 表现出更高的活性和更好的重复使用效率，在 60min 和 90min 后具有更高的价值。在所有研究条件下都观察到了肽的合成。分析（DPPH、β-胡萝卜素/亚油酸、FRAP）证实了固定化酶生成肽的抗氧化潜力。然而，固定在 ACG50 和 ACG100 中的酶与更长的水解时间相结合，允许形成具有抗氧化能力的肽，其能力大于或等于游离酶生成的肽，尽管酶活性降低。
