Cooperative Innovation Center of Industrial Fermentation (Ministry of Education & Hubei Province), Hubei University of Technology, Wuhan, 430068, China; School of Life and Health Sciences, Hubei University of Technology, Wuhan, 430068, China.
School of Modern Industry for Selenium Science and Engineering, Wuhan Polytechnic University, Wuhan, 430068, China.
Carbohydr Polym. 2025 Jan 1;347:122757. doi: 10.1016/j.carbpol.2024.122757. Epub 2024 Sep 19.
β-Galactosidase (lactase) plays a crucial role as a dietary supplement in managing lactose intolerance. Here, the catalytic activity of lactase was successfully activated for the first time through complexation with water-extractable β-glucans from highland barley (WHBG). Under simulated gastric/small intestinal digestive conditions, WHBG and lactase spontaneously formed complexes, resulting in a remarkable increase in catalytic activity up to 172.6 %. Structural analyses revealed that the incorporation of WHBG caused partial unfolding of lactase, thereby exposing its hydrophobic regions with active sites, and the electrostatic and hydrophobic interactions between the two played pivotal roles. Meanwhile, according to microstructure and particle size analyses, the dissociation of aggregates and the re-distribution of lactase molecules were also observed. Consequently, the enzyme-substrate contact was promoted, and the hydrolysis efficiency of complexed lactase in the digestion of lactose in milk was superior to that of native lactase. Notably, among WHBG30/50/70 obtained by continuous fractionation of WHBG with 30 %/50 %/70 % ethanol, WHBG70 exhibited the lowest molecular weights and size, and the highest negative ζ-potential, potentially contributing to its superior activation abilities on lactase. These findings challenge the traditional view of polysaccharides as enzyme inhibitors and highlight their potential for diverse applications.
β-半乳糖苷酶(乳糖酶)作为膳食补充剂在乳糖不耐受管理中起着至关重要的作用。在这里,首次通过与来自青稞的可提取水β-葡聚糖(WHBG)络合成功激活了乳糖酶的催化活性。在模拟胃/小肠消化条件下,WHBG 和乳糖酶自发形成复合物,催化活性显著提高了 172.6%。结构分析表明,WHBG 的加入导致乳糖酶部分展开,从而暴露出其具有活性位点的疏水区,两者之间的静电和疏水相互作用起着关键作用。同时,根据微观结构和粒径分析,还观察到聚集物的解离和乳糖酶分子的重新分布。因此,促进了酶-底物的接触,复合乳糖酶在牛奶中乳糖消化的水解效率优于天然乳糖酶。值得注意的是,在 WHBG 用 30%/50%/70%乙醇连续分级得到的 WHBG30/50/70 中,WHBG70 表现出最低的分子量和粒径,以及最高的负 ζ-电位,这可能有助于其对乳糖酶的优越激活能力。这些发现挑战了多糖作为酶抑制剂的传统观点,并强调了它们在各种应用中的潜力。