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Wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus: substrate specificity and biotechnological potential for wax ester production

机译:来自Marinobacterscoclasticus的蜡合作酶MHWS2:蜡酯产生的底物特异性和生物技术潜力

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摘要

Wax synthases are involved in the biosynthesis of wax esters, lipids with great industrial potential. Here, we heterologously expressed the native wax synthase MhWS2 from Marinobacter hydrocarbonoclasticus in Saccharomyces cerevisiae and performed comprehensive analysis of its substrate specificity. The enzyme displayed high wax synthase (but no diacylglycerol acyltransferase) activity both in vivo and in vitro. In the presence of exogenous fatty alcohol, wax esters accounted for more than 57% of total yeast lipids. In vitro, MhWS2 produced wax esters with most of the tested substrates, showing the highest activity with 14:0-, 18:1-, 18:0-, 12:0-, and 16:0-CoA together with saturated C10-C16 fatty alcohols. Co-expression with genes encoding fatty acyl reductases resulted in the accumulation of C26-C36 wax esters. Altogether, our results provide a detailed characterization of MhWS2 which should be useful in the development of strategies for producing wax esters in various expression systems.
机译:蜡合成酶参与蜡酯的生物合成,脂质具有巨大的工业潜力。在这里,我们在酿酒酵母中的含有烃类嗜烃基皮序中异常表达了本地蜡合酶MHWS2,并对其底物特异性进行了综合分析。酶在体内和体外显示高蜡合酶(但没有二酰基甘油酰基转移酶)活性。在外源脂肪醇存在下,蜡酯占总酵母脂质的57%以上。在体外,MHWS2产生具有大部分测试基材的蜡酯,显示最高活性,最高活性为14:0-,18:1-,18:0-,12:0-和16:0-CoA以及饱和C10- C16脂肪醇。与编码脂肪酰化还原酶的基因的共表达导致C26-C36蜡酯的积累。完全相同,我们的结果提供了MHWS2的详细表征,在制定各种表达系统中生产蜡酯的策略应该有用。

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