Gupta M N
Chemistry Department, Indian Institute of Technology, Delhi.
Eur J Biochem. 1992 Jan 15;203(1-2):25-32. doi: 10.1111/j.1432-1033.1992.tb19823.x.
Enzyme catalysis in organic solvents is being increasingly used for a variety of applications. Of special interest are the cases in which the medium is predominantly non-aqueous and contains little water. A display of enzyme activity, even in anhydrous solvents (water less than 0.02% by vol.), perhaps reflects that the minimum necessity for water is for forming bonds with polar amino acids on the enzyme surface. The rigidity of enzyme structure at such low water content results in novel substrate specificities, pH memory and the possibility of techniques such as molecular imprinting. Limited data indicates that, while enhanced thermal stability invariably results, the optimum temperature for catalysis may not change. If true in general, this enhanced thermostability would have extremely limited benefits. Medium engineering and biocatalyst engineering are relevant techniques to improve the efficiency and stability of enzymes in such low water systems. Most promising, as part of the latter, is the technique of protein engineering. Finally, this review provides illustrations of applications of such systems in the diverse areas of organic synthesis, analysis and polymer chemistry.
有机溶剂中的酶催化正越来越多地用于各种应用。特别令人感兴趣的是那些介质主要为非水且含水量很少的情况。即使在无水溶剂(水含量低于0.02%体积分数)中酶仍表现出活性,这或许反映出对水的最低需求是与酶表面的极性氨基酸形成键。在如此低的含水量下酶结构的刚性导致了新的底物特异性、pH记忆以及诸如分子印迹等技术的可能性。有限的数据表明,虽然热稳定性总是增强,但催化的最佳温度可能不变。如果总体上确实如此,这种增强的热稳定性带来的益处将极为有限。介质工程和生物催化剂工程是提高酶在这种低水体系中的效率和稳定性的相关技术。作为后者的一部分,最有前景的是蛋白质工程技术。最后,本综述举例说明了此类体系在有机合成、分析和聚合物化学等不同领域的应用。