Enzyme immobilization assisted by protein assemblies for highly efficient biocatalysis in organic systems

ZHAI Tingting; GU Hongzhou; FAN Chunhai

doi:10.12211/2096-8280.2022-015

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Enzyme immobilization assisted by protein assemblies for highly efficient biocatalysis in organic systems

Comment | 更新时间：2025-03-20

- Enzyme immobilization assisted by protein assemblies for highly efficient biocatalysis in organic systems
- Synthetic Biology Journal Vol. 3, Issue 2, Pages: 256-259(2022)
- 作者机构：
  
  上海交通大学化学化工学院，上海 200240
- 作者简介：
- 基金信息：
- DOI：10.12211/2096-8280.2022-015
  CLC： Q81
- Received：03 March 2022，
  
  Revised：2022-03-13，
  
  Published：30 April 2022
- 稿件说明：
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翟婷婷，顾宏周，樊春海. 蛋白质组装体辅助的酶固定：精准构建有机相高效生物催化剂［J］. 合成生物学， 2022， 3（2）： 256-259

ZHAI Tingting， GU Hongzhou， FAN Chunhai. Enzyme immobilization assisted by protein assemblies for highly efficient biocatalysis in organic systems［J］. Synthetic Biology Journal， 2022， 3（2）： 256-259
翟婷婷，顾宏周，樊春海. 蛋白质组装体辅助的酶固定：精准构建有机相高效生物催化剂［J］. 合成生物学， 2022， 3（2）： 256-259 DOI： 10.12211/2096-8280.2022-015.

ZHAI Tingting， GU Hongzhou， FAN Chunhai. Enzyme immobilization assisted by protein assemblies for highly efficient biocatalysis in organic systems［J］. Synthetic Biology Journal， 2022， 3（2）： 256-259 DOI： 10.12211/2096-8280.2022-015.

摘要

酶作为一类高效的生物催化剂，是化学工业生产中的主要驱动力之一，被广泛用于精细化工、食品加工和医药生产等多个领域。然而，酶的三维活性结构极易被有机溶剂破坏，严重阻碍了其在含有机溶剂的工业生产中的应用。如何保持有机溶剂催化反应体系中的酶活性，是有机相工业生产中亟待解决的问题。酶的固定化被认为是保留酶稳定性的有效手段之一。近期，张先恩和门冬团队利用具有自组装特性的酵母朊蛋白Sup35为基质，构建了一种兼具亲疏水复合界面结构的Januvia转氨酶（JTA）纳米线。JTA纳米线在多种有机溶剂体系中呈现出优异的催化活性，且具有良好的热稳定性和pH稳定性。该工作为有机体系中的酶催化提供了一种优异的酶固定策略，拓宽了酶催化在有机相工业生产中的应用前景。

Abstract

Enzymes have been regarded as key players in producing chemicals

including fine

chemical products

food and pharmaceuticals

but the poor stability of three-dimensional folding structures with the enzymes impede their applications in organic systems. Maintaining enzymatic activities in organic solvents has becoming one of the urgent issues in enzyme-dependent industrial applications. Interfacial immobilization is an attractive strategy for stabilizing the structures of enzymes. Recently

an elegant strategy has been reported for constructing organic Januvia transaminase nanowires (JTAnw) with high stability in the organic system. Using the self-assembly domain of the amyloid protein Sup35 as a hydrophobic support

a unique “dry and wet” interface is constructed for JTAnws

and this interface can effectively enhance Januvia transaminase

s catalytic activity

thermal stability and pH stability in different organic solvents. The work provides a smart enzyme-immobilization strategy for improving enzymes

catalysis performance in organic systems

which would expand their applications for biocatalysis in organic solvents.

关键词

Keywords

references

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RUEDA N , DOS SANTOS J C S , ORTIZ C , et al . Chemical modification in the design of immobilized enzyme biocatalysts: drawbacks and opportunities [J ] . The Chemical Record , 2016 , 16 ( 3 ): 1436 - 1455 .

KIM K H , KO D K , KIM Y T , et al . Protein-directed self-assembly of a fullerene crystal [J ] . Nature Communications , 2016 , 7 : 11429 .

LUO Q , HOU C X , BAI Y S , et al . Protein assembly: versatile approaches to construct highly ordered nanostructures [J ] . Chemical Reviews , 2016 , 116 ( 22 ): 13571 - 13632 .

WEI C H , ZHOU J , LIU T G , et al . Self-assembled enzymatic nanowires with a “dry and wet” interface improve the catalytic performance of Januvia transaminase in organic solvents [J ] . ACS Catalysis , 2022 , 12 ( 1 ): 372 - 382 .

NELSON R , SAWAYA M R , BALBIRNIE M , et al . Structure of the cross- β spine of amyloid-like fibrils [J ] . Nature , 2005 , 435 ( 7043 ): 773 - 778 .

CARLSSON A C C , SCHOLFIELD M R , ROWE R K , et al . Increasing enzyme stability and activity through hydrogen bond-enhanced halogen bonds [J ] . Biochemistry , 2018 , 57 ( 28 ): 4135 - 4147 .

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