Evidence map›Paper›PMID 40354901›Full record

ReviewBiotechnology advances2025

Enzyme miniaturization: Revolutionizing future biocatalysts.

Ning Ding, Yaoyukun Jiang, Sangsin Lee, Zihao Cheng, Xinchun Ran, Yujing Ding, Robbie Ge, Yifei Zhang, Zhongyue J Yang

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biotechnology advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Ning DingDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235, United States; Center for Structural Biology, Vanderbilt University, Nashville, TN 37235, United States. Electronic address: ning.ding@vanderbilt.edu.
Yaoyukun JiangDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235, United States; Department of Chemistry and California Institute for Quantitative Biosciences, University of California-Berkeley, Berkeley, CA 94720, United States.
Sangsin LeeDepartment of Genetics, Stanford University, Stanford, CA 94305, United States.
Zihao ChengDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235, United States.
Xinchun RanDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235, United States.
Yujing DingState Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing 100029, China; Beijing Advanced Innovation Center for Soft Matter Science and Engineering, Beijing University of Chemical Technology, Beijing 100029, China.
Robbie GeDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235, United States.
Yifei ZhangState Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing 100029, China; Beijing Advanced Innovation Center for Soft Matter Science and Engineering, Beijing University of Chemical Technology, Beijing 100029, China. Electronic address: yifeizhang@mail.buct.edu.cn.
Zhongyue J YangDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235, United States; Center for Structural Biology, Vanderbilt University, Nashville, TN 37235, United States. Electronic address: zhongyue.yang@vanderbilt.edu.

Funding

Developing Computational Tools for Predicting and Designing Function-Enhancing Enzyme VariantsR35GM146982 · NIGMS · VANDERBILT UNIVERSITY · PI Zhongyue Yang · 2022 to 2026
$1.8M
NIGMS NIH HHS R35 GM146982
6 · The paper itself

Abstract

Enzyme miniaturization offers a transformative approach to overcome limitations posed by the large size of conventional enzymes in industrial, therapeutic, and diagnostic applications. However, the evolutionary optimization of enzymes for activity has not inherently favored compact structures, creating challenges for modern applications requiring smaller catalysts. In this review, we surveyed the advantages of miniature enzymes, including enhanced expressivity, folding efficiency, thermostability, and resistance to proteolysis. We described the applications of miniature enzymes as industrial catalysts, therapeutic agents, and diagnostic elements. We highlighted strategies such as genome mining, rational design, random deletion, and de novo design for achieving enzyme miniaturization, integrating both computational and experimental techniques. By investigating these approaches, we aim to provide a framework for advancing enzyme engineering, emphasizing the unique potential of miniature enzymes to revolutionize biocatalysis, gene therapy, and biosensing technologies.

Indexed as

BiocatalysisEnzymesMiniaturizationProtein EngineeringBiosensing TechniquesBiotechnologyHumansEnzymesBiocatalysisBiomedicineBiosensingEnzyme engineeringEnzyme expressionEnzyme miniaturization

Identifiers

PMID40354901
PMCPMC12226312

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.