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Related Experiment Video

Updated: Jun 19, 2026

High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits

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Published on: September 20, 2016

Engineered amadoriase II exhibiting expanded substrate range.

Jing Zheng¹, Hong Guan, Lihua Xu

¹Department of Chemical Engineering, Tsinghua University, One Tsinghua Garden Road, Beijing, 100084, China.

Applied Microbiology and Biotechnology

|November 6, 2009

Summary

This summary is machine-generated.

Researchers engineered fructosyl amine oxidases (FAOXs) to break down larger Amadori compounds, expanding their potential use in diagnostics and therapeutics. The new mutant enzyme shows improved activity on complex substrates like gravy stains.

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Published on: November 23, 2016

Area of Science:

Biochemistry
Enzyme Engineering
Biotechnology

Background:

Amadori compounds are widespread in biological systems and food, linked to diabetic complications and aging.
Fructosyl amine oxidases (FAOXs) are enzymes that degrade Amadori products.
Current FAOXs have limited substrate specificity, restricting their practical applications.

Purpose of the Study:

To engineer Aspergillus fumigatus amadoriase II to broaden its substrate range.
To develop FAOXs capable of acting on larger glycated molecules.

Main Methods:

Utilized a heat-inducible autolytic vector for enzyme engineering.
Employed fructosyl-polylysine as an intermediate-sized model substrate.
Performed two rounds of directed evolution to enhance enzyme activity.

Main Results:

Developed a mutant enzyme (SII-82) with an 8.78-fold increase in activity towards fructosyl-polylysine.
The engineered enzyme demonstrated significantly improved performance on real gravy stains.
Identified key mutations providing insights into substrate-binding pocket modification.

Conclusions:

Demonstrated the feasibility of engineering FAOXs to accept larger substrates.
The mutant SII-82 shows promise for applications in diagnostics, therapeutics, and detergents.
The engineered enzyme can serve as a foundation for future enzyme development.