Rapuano Roberta, Graziano Giuseppe
Dipartimento di Scienze e Tecnologie, Università del Sannio, Via Francesco de Sanctis snc, 82100 Benevento, Italy.
Microorganisms. 2022 Jun 6;10(6):1161. doi: 10.3390/microorganisms10061161.
Enzymes purified from psychrophilic microorganisms prove to be efficient catalysts at low temperatures and possess a great potential for biotechnological applications. The low-temperature catalytic activity has to come from specific structural fluctuations involving the active site region, however, the relationship between protein conformational stability and enzymatic activity is subtle. We provide a survey of the thermodynamic stability of globular proteins and their rationalization grounded in a theoretical approach devised by one of us. Furthermore, we provide a link between marginal conformational stability and protein flexibility grounded in the harmonic approximation of the vibrational degrees of freedom, emphasizing the occurrence of long-wavelength and excited vibrations in all globular proteins. Finally, we offer a close view of three enzymes: chloride-dependent α-amylase, citrate synthase, and β-galactosidase.
从嗜冷微生物中纯化得到的酶在低温下是高效催化剂，具有巨大的生物技术应用潜力。然而，低温催化活性必须源于涉及活性位点区域的特定结构波动，蛋白质构象稳定性与酶活性之间的关系很微妙。我们综述了球状蛋白质的热力学稳定性，并基于我们其中一人设计的理论方法对其进行了合理化解释。此外，我们基于振动自由度的简谐近似，建立了边缘构象稳定性与蛋白质灵活性之间的联系，强调了所有球状蛋白质中长波长和激发振动的存在。最后，我们详细介绍了三种酶：氯离子依赖性α-淀粉酶、柠檬酸合酶和β-半乳糖苷酶。
