关键词: Bioprospecting Enzyme catalysis Protein dynamics Psychrophilicity Thermodynamic stability

来  源:   DOI:10.1016/j.bbadva.2023.100104   PDF(Pubmed)

Abstract:
Enzymes from psychrophilic (cold-loving) organisms have attracted considerable interest over the past decades for their potential in various low-temperature industrial processes. However, we still lack large-scale commercialization of their activities. Here, we review their properties, limitations and potential. Our review is structured around answers to 5 central questions: 1. How do cold-active enzymes achieve high catalytic rates at low temperatures? 2. How is protein flexibility connected to cold-activity? 3. What are the sequence-based and structural determinants for cold-activity? 4. How does the thermodynamic stability of psychrophilic enzymes reflect their cold-active capabilities? 5. How do we effectively identify novel cold-active enzymes, and can we apply them in an industrial context? We conclude that emerging screening technologies combined with big-data handling and analysis make it reasonable to expect a bright future for our understanding and exploitation of cold-active enzymes.
摘要:
在过去的几十年中,来自嗜冷(嗜冷)生物的酶因其在各种低温工业过程中的潜力而引起了极大的兴趣。然而,我们仍然缺乏他们活动的大规模商业化。这里,我们审查他们的财产,限制和潜力。我们的评论围绕5个中心问题的答案进行:1.冷活性酶如何在低温下实现高催化速率?2。蛋白质的灵活性如何与冷活动相关?3.冷活性的基于序列和结构决定因素是什么?4.嗜冷酶的热力学稳定性如何反映其冷活性能力?5。我们如何有效地识别新型冷活性酶,我们可以在工业环境中应用它们吗?我们得出结论,新兴的筛选技术与大数据处理和分析相结合,可以合理地期望我们对冷活性酶的理解和利用有光明的未来。
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