Instituto de Agroquímica y Tecnología de Alimentos, CSIC, Valencia, Spain.
Instituto de Agroquímica y Tecnología de Alimentos, CSIC, Valencia, Spain; Departamento de Bioquímica y Biología Molecular, Universidad de Valencia, Spain.
Int J Biol Macromol. 2020 May 15;151:602-608. doi: 10.1016/j.ijbiomac.2020.02.115. Epub 2020 Feb 12.
Thermostable β-galactosidase (TmLac) has been immobilized as hybrid inorganic-protein nanoflowers using salts of Cu, Mn, Zn, Co and Ca as the inorganic component. The incorporation efficiency of enzyme into the nanoflowers was higher than 95% for a protein concentration of 0.05 mg/mL. The structure, activity and recyclability of the nanoflowers with different chemical composition were analyzed. Ca, Mn and Co nanoflowers showed a level of lactase activity equivalent to their same content of free enzyme. Cunanoflowers showed only marginal enzyme activity in agreement with the inhibitory effect of this cation on the enzyme. TmLac nanoflowers provide an efficient methodology for enzyme immobilization and recyclability. TmLac-Ca nanoflowers presented the best properties for lactose hydrolysis both in buffered and in milk, and could be reused in five consecutive cycles.
热稳定β-半乳糖苷酶（TmLac）已通过使用 Cu、Mn、Zn、Co 和 Ca 的盐作为无机成分固定化为杂化无机-蛋白质纳米花。对于 0.05mg/mL 的蛋白质浓度，酶的掺入效率高于 95%。分析了具有不同化学成分的纳米花的结构、活性和可回收性。Ca、Mn 和 Co 纳米花的乳糖酶活性与游离酶的相同含量相当。Cu 纳米花的酶活性仅略有增加，这与该阳离子对酶的抑制作用一致。TmLac 纳米花为酶固定化和可回收性提供了一种有效的方法。TmLac-Ca 纳米花在缓冲液和牛奶中都具有最佳的乳糖水解性能，并且可以在五个连续循环中重复使用。
