糖基转移酶(GTs)是一类广泛的转移糖部分的酶,在细菌胞外多糖(EPS)生物聚合物的合成中起关键作用。近年来,在制药中观察到对细菌EPS的需求增加,食物,和其他行业。EPS的应用很大程度上取决于它们的热稳定性,因为任何工业应用主要依赖于缓慢的热降解。把这件事放在上下文中,基于生长温度(中温,嗜热细菌,和超嗜热菌)被认为是结构功能关系的计算机模拟分析。从目前的研究来看,观察到GT的结构完整性从中温菌到嗜热菌到超嗜热菌显著增加。相比之下,结构可塑性朝着中温生物的方向相反。这种有趣的温度依赖性结构特性指导了GT-UDP-葡萄糖相互作用,使得嗜热细菌最终证明了更好的结合亲和力(-5.57至-10.70),氢键数量增加(355)和稳定的氨基酸(Phe,阿拉,Glu,Tyr,andSer).这项研究的结果可能直接利用嗜热细菌来源的GT作为工业水平细菌多糖生产的最佳选择。
Glycosyltransferase (GTs) is a wide class of enzymes that transfer sugar moiety, playing a key role in the synthesis of bacterial exopolysaccharide (EPS) biopolymer. In recent years, increased demand for bacterial EPSs has been observed in pharmaceutical, food, and other industries. The application of the EPSs largely depends upon their thermal stability, as any industrial application is mainly reliant on slow thermal degradation. Keeping this in context, EPS producing GT enzymes from three different bacterial sources based on growth temperature (mesophile, thermophile, and hyperthermophile) are considered for in silico analysis of the structural-functional relationship. From the present
study, it was observed that the structural integrity of GT increases significantly from mesophile to thermophile to hyperthermophile. In contrast, the structural plasticity runs in an opposite direction towards mesophile. This interesting temperature-dependent structural property has directed the GT-UDP-glucose interactions in a way that thermophile has finally demonstrated better binding affinity (-5.57 to -10.70) with an increased number of hydrogen bonds (355) and stabilizing amino acids (Phe, Ala, Glu, Tyr, and Ser). The results from this
study may direct utilization of thermophile-origin GT as best for industrial-level bacterial polysaccharide production.