Use of certain alcohol ethoxylates to maintain protease stability in the presence of anionic surfactants
Use of certain alcohol ethoxylates to maintain protease stability in the presence of anionic surfactants
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DOI：
10.1007/s11743-002-0198-9
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发表时间：
2002-01-01
影响因子：
1.6
通讯作者：
Britton, LN
中科院分区：
文献类型：
--
作者：
Russell, GL;Britton, LN
阴离子表面活性剂，包括直链烷基苯磺酸盐 (LAS)，已知会降低洗涤剂蛋白酶的稳定性，可能是通过加速自蛋白水解过程。因此，含酶重垢液体衣物洗涤剂 (HDL) 中的蛋白酶保质期通常通过添加稳定剂、限制干扰阴离子的水平或通过使用更相容的阴离子（例如醇乙氧基硫酸盐 (AES)）来维持。本研究检验了基于 LAS 并含有不同醇乙氧基化物 (AE) 的 HDL 配方中 Savinase(R) 去污剂蛋白酶的稳定性，以防止蛋白酶失活。剂量响应曲线表明，除 AES 外，所有常用的阴离子表面活性剂都会促进蛋白酶活性的损失。在具有等百分比 LAS 和 AE 组成的 HDL 制剂中，发现所选 AE 的结构对蛋白酶稳定性具有深远影响，包含链长大于或等于 C(14) 且乙氧基化水平 > 70% 的 AE 会导致更高的蛋白酶稳定性。可以配制含有 LAS 和这些保护性 AE 的 HDL，以实现与模拟商业产品相匹配的蛋白酶稳定性。与多羟基稳定剂不同，AE 本身不会给蛋白酶带来额外的稳定性。 “保护性”AE 的稳定作用更有可能是由于 LAS 对蛋白酶的可用性降低所致。
Anionic surfactants, including linear alkylbenzene sulfonate (LAS), are known to decrease the stability of detergent proteases, possibly by hastening autoproteolytic processes. Thus, protease shelf life in enzyme-containing, heavy-duty liquid laundry detergents (HDL) is typically maintained by adding stabilizers, by limiting the level of interfering anionics, or by utilizing more compatible anionics, such as a alcohol ethoxysulfates (AES). This study examines the stability of Savinase(R) detergent protease in HDL formulations based on LAS and containing different alcohol ethoxylates (AE) for protection against protease inactivation. Dose response curves demonstrated that all commonly used anionic surfactants exceptAES promote loss of protease activity. In HDL formulations with equal percentage compositions of LAS and AE, the structure of the selected AE was found to have a profound influence on protease stability, Inclusion of AE with chain length greater than or equal toC(14) and ethoxylate levels >70% resulted in greater protease stability. HDL containing LAS and these protective AE could be formulated to achieve protease stability matching those of simulated commercial products. Unlike polyhydric stabilizers, the AE by themselves confer no additional stability to the protease. It is more likely that the stabilizing effect of the "protective" AE is due to decreased availability of LAS to the protease.