The active site of Candida rugosa lipase (CRL) is mainly hydrophilic on its external face and hydrophobic on the internal side, and calix[n]arene-based surfactants form complexes with protein residues or with strong hydrogen bonds to open up the lid. Therefore, the activity of lipase persists for a long time. In this work, a series of cyclic and acyclic anionic surfactants (sodium dodecyl sulfate (SDS), p-sulfonatocalix[4]arene, and p-sulfonatocalix[8]arene) and zwitterionic surfactants (l-proline and l-proline derivative of calix[4]arene) were used to examine the relationship between the surfactants’ molecular structures and their effects on the hydrolytic activity of CRL. We explored the effects of different surfactant concentrations, ring effects, and mixing times on CRL activity and several kinetic parameters. The results demonstrated that cyclic compounds were more effective than linear structures for increasing CRL activity and the highest enzyme activity was obtained by the addition of the calix[4]-l-proline derivative. This zwitterionic compound (calix[4]-l-proline derivative) maintains the active center of enzyme and conformation by enabling electrostatic interactions and hydrogen bonding with both the acidic and basic amino acid groups in the structure of the enzyme. The results indicated that, compared with the other surfactants, activating CRL with calix[4]-l-proline resulted in hyperactivation at all concentrations (a relative increase of 230%).

皱纹假丝酵母脂肪酶（CRL）的活性位点主要是外表面亲水，内表面疏水，杯[ n ]芳烃基表面活性剂与蛋白质残基或强氢键形成复合物，打开盖子。因此，脂肪酶的活性会持续很长时间。在这项工作中，一系列环状和非环状阴离子表面活性剂（十二烷基硫酸钠（SDS）、对磺化杯[4]芳烃和对磺化杯[8]芳烃）和两性离子表面活性剂（l-脯氨酸和l杯[4]芳烃的-脯氨酸衍生物）被用来研究表面活性剂的分子结构及其对CRL水解活性的影响之间的关系。我们探讨了不同表面活性剂浓度、环效应和混合时间对 CRL 活性和几个动力学参数的影响。结果表明环状化合物比线性结构更有效地提高CRL活性，并且通过加入杯[4] -l-脯氨酸衍生物获得最高的酶活性。这种两性离子化合物（calix[4] -l-脯氨酸衍生物）通过使酶结构中的酸性和碱性氨基酸基团产生静电相互作用和氢键来维持酶的活性中心和构象。结果表明，与其他表面活性剂相比，用杯[4] -l-脯氨酸激活CRL导致所有浓度的过度激活（相对增加230%）。