YKI, Institute for Surface Chemistry, Box 5607, SE-114 86 Stockholm, Sweden.
J Colloid Interface Sci. 2010 Mar 1;343(1):359-65. doi: 10.1016/j.jcis.2009.11.014. Epub 2009 Nov 10.
Lipase from Thermomyces lanuginosus has been immobilized within particulate mesoporous silica carriers, with either hydrophilic or hydrophobic supporting surfaces, produced by the newly developed emulsion and solvent evaporation (ESE) method. The Michaelis-Menten model was used to calculate the parameters related to the enzymatic activity of lipase i.e. the turnover number, k(cat), and the specific activity. The specific activity was improved by immobilization of lipase onto the hydrophobic support, compared to lipase immobilized onto the hydrophilic support and lipase free in solution. The enhanced enzymatic activity of lipase onto a hydrophobic support was attributed to interfacial activation of the Thermomyces lanuginosus lipase when it is attached to a hydrophobic surface and a reduced denaturation. Confocal scanning laser microscopy (CLSM) studies, of fluorescently tagged lipase, showed that leakage of the lipase from the mesoporous particles was limited to an initial period of only a few hours. Both the rate and the amount of lipase leached were reduced when the lipase was immobilized onto the hydrophobic support.
脂肪酶从Thermomyces lanuginosus已被固定在颗粒状介孔硅载体内，具有亲水性或疏水性支撑表面，由新开发的乳液和溶剂蒸发（ESE）方法产生。米氏模型被用来计算与脂肪酶酶活性相关的参数，即 turnover number，k（cat）和比活性。与固定在亲水性载体上的脂肪酶和游离在溶液中的脂肪酶相比，脂肪酶固定在疏水性载体上提高了比活性。脂肪酶在疏水性载体上的增强酶活性归因于Thermomyces lanuginosus 脂肪酶附着在疏水性表面时的界面激活和变性减少。荧光标记的脂肪酶的共焦扫描激光显微镜（CLSM）研究表明，脂肪酶从介孔颗粒中的泄漏仅限于最初的几个小时。当脂肪酶固定在疏水性载体上时，脂肪酶的泄漏速度和量都减少了。
