Augmenting off-the-shelf enzyme activities by multiple folds with a supramolecular complex additive

Enzymes are commonly used industrial reagents, and enhancement of their activity is often pursued to make them more attractive reagents. Here, we discovered that simply adding two chemical additives can augment many enzyme activities above their native range in their usual reaction buffers, leading to around 1.5–40 times higher reaction rates and product yields. The augmenting system comprises a zwitterionic bile salt derived detergent and a per-aminated cyclodextrin, forming a dynamic supramolecular system for in perpetuum protein folding. Our discovery provides an additional dimension to augment protein functions independent of other parameters and suggests certain solutes may provide near-universal modulation of protein functions beyond the commonly considered electrolytes and solvents. • Simply adding two chemicals can augment enzyme activity by 1.5-40x. • The augmentation broadly applies to various enzymes and reaction conditions. • Our approach represents a new approach to increase enzyme activity.

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Publication Details

Journal
Green Chemical Engineering
Published
2025-08-01
DOI
https://doi.org/10.1016/j.gce.2025.08.001
Primary Topic
Supramolecular Self-Assembly in Materials
Type
article
Field-Weighted Citation Impact
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article

Augmenting off-the-shelf enzyme activities by multiple folds with a supramolecular complex additive

Tin Yan Wong, Chun Ngo Yau, H. M. Lai, Pui Lam Tsoi
Green Chemical Engineering
Supramolecular Self-Assembly in Materials
article

Augmenting off-the-shelf enzyme activities by multiple folds with a supramolecular complex additive

Tin Yan Wong, Chun Ngo Yau, H. M. Lai, Pui Lam Tsoi
article en

Abstract

Enzymes are commonly used industrial reagents, and enhancement of their activity is often pursued to make them more attractive reagents. Here, we discovered that simply adding two chemical additives can augment many enzyme activities above their native range in their usual reaction buffers, leading to around 1.5–40 times higher reaction rates and product yields. The augmenting system comprises a zwitterionic bile salt derived detergent and a per-aminated cyclodextrin, forming a dynamic supramolecular system for in perpetuum protein folding. Our discovery provides an additional dimension to augment protein functions independent of other parameters and suggests certain solutes may provide near-universal modulation of protein functions beyond the commonly considered electrolytes and solvents. • Simply adding two chemicals can augment enzyme activity by 1.5-40x. • The augmentation broadly applies to various enzymes and reaction conditions. • Our approach represents a new approach to increase enzyme activity.

Green Chemical Engineering
Chinese University of Hong Kong (HK)
Openalex Percentile: Top 87%
Supramolecular Self-Assembly in Materials
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