高效地固定热友拉姆诺酶双网混合凝,具有高酶活性和稳定性
Wenli Xia1, Jingcong Xie2, Linguo Zhao1
1National Key Laboratory for the Development and Utilization of Forest Food Resources, Nanjing Forestry University, Nanjing 210037, China; Jiangsu Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Jiangsu Key Lab of Biomass-Based Green Fuels and Chemicals, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, China.
Bioorganic chemistry
|August 5, 2025
概括
一种新的双网络混合凝有效地使热友性酶停滞不前,提高了它们的稳定性和可用于高温生物转换的可重复使用性. 这种新的载体材料显著提高了工业应用中的酶活性和寿命.
科学领域:
- 生物技术和生物催化剂
- 材料科学用于酶固定化
- 蛋白质工程和酶技术技术
背景情况:
- 热友性酶为生物转化提供了诸如高催化活性和热稳定性等优势.
- 一个主要的限制是缺乏适合的固定材料,既耐热又可重复使用.
- 这阻碍了热友酶在工业过程中的高效和重复使用.
研究的目的:
- 开发一种新的双网络混合凝载体,用于耐热和可重复使用的热友酶的固定.
- 调查这种混合凝在增强α-rhamnosidase IagRha的稳定性,活性和可重复使用性方面的有效性.
- 评估固定酶在工业生物转化应用中的潜力.
主要方法:
- 通过使用烯胺 (AM) 和藻酸盐 (SA) 合成了一种双网络混合凝,其度优化 (5% AM,2% SA).
- 凝结构是通过烯胺交联形成的,其次是Ca2+浸入,以与SA产生离子键,增强热稳定性和酶负荷.
- 固定式α-rhamnosidase (AM-SA-IagRha) 的特征是活动恢复,Vmax,热稳定性,可重复使用性和存储稳定性.
主要成果:
- 混合凝固定实现了93.65%的酶活性恢复,并显著增强了酶特性.
- 固定IagRha (AM-SA-IagRha) 显示Vmax (7.06U/mg) 增加1.34倍,半衰期在90°C (99.0分钟) 时长1.57倍.
- AM-SA-IagRha表现出优异的可重复使用性 (85.63%的活性在20个循环后) 和存储稳定性 (90.16%的活性在4°C下30天后),显著提高了鲁丁和Epimedin C. 的生产力.
结论:
- 开发的AM-SA双网络混合凝是一种高效且可重复使用的载体,用于热友酶固定.
- 这种固定化策略大大提高了酶的热稳定性,催化效率和操作稳定性.
- 对于工业应用来说,AM-SA-IagRha显著有前途,特别是在高温生物转化过程中.
相关概念视频
Enzymes
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Introduction to Mechanisms of Enzyme Catalysis
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...


