α-淀粉酶低温适应性分子机制的研究进展

Advanced in Molecular Mechanism of Adaptability of Cold-Adapted α-Amylase

低温酶由于在低温下仍能保持高催化活性而具有很高的工业应用价值。而关于低温酶是如何适应低温环境以及在低温下如何保持高催化活性等问题,同样引起了各国科学家们的广泛关注。其中低温α-淀粉酶是在结构和功能方面研究得最为透彻的酶,它也是第一个被结晶的低温酶,其热、动力学特征已通过内荧光法、圆二色性和差示扫描量热法等进行了深入研究。建立在三维结构分析和热力学特征研究的基础上,科学家们目前正尝试着解开低温酶的低温适应性之谜。对低温α-淀粉酶的研究进展作一简要的综述。

Cold-adapted enzymes possess highly industrial application values due to their high catalytic activity even at very low temperature, Recently, about how cold-adapted enzymes keep their high catalytic activity to low temperature environment have brought about international scientists＇ extensive attentions, Among them cold-adapted α-amylase was the one that has been studied thoroughly in the relation of its structure and function, it is also the first one that was crystallized and has been carried out its thermal stability by intrinsic fluorescence, circular dichroism, and differential scanning calorimetry. Based on 3D structure analysis and thermodynamic feature research, scientists are now trying to illustrate the adaptability mechanism of cold-adapted enzyme to cold environment. A brief review of recent progress of cold-adapted α-amylase in this field is given in this paper.