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Updated: Jul 6, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

Keratin transamidation.

Jeanette M Cardamone¹

¹US Department of Agriculture, Agricultural Research Service, Eastern Regional Research Center, 600 East Mermaid Lane, Wyndmoor, PA 19038, USA. jan.cardamone@ars.usda.gov

International Journal of Biological Macromolecules

|April 9, 2008

Summary

This summary is machine-generated.

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Keratin capped silver nanoparticles--synthesis and characterization of a nanomaterial with desirable handling properties.

Colloids and surfaces. B, Biointerfaces·2011

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Microbial transglutaminase (mTGase) enables low molecular weight keratin to self-crosslink, enhancing wool fabric properties. This protein crosslinking improves wool strength and dimensional stability.

Area of Science:

Biochemistry
Materials Science
Textile Chemistry

Background:

Keratin, a key structural protein in wool, can be modified for improved textile applications.
Microbial transglutaminase (mTGase) is an enzyme known to catalyze protein crosslinking reactions.

Purpose of the Study:

To investigate the self-crosslinking of low molecular weight keratin using mTGase.
To evaluate the efficacy of this self-crosslinking for wool fabric treatment.

Main Methods:

Alkaline hydrolysis of wool to produce low molecular weight keratin.
Amino acid analysis to confirm glutamine and lysine content.
Enzymatic treatment with mTGase.
Gel electrophoresis and FTIR spectroscopy to analyze crosslinking.

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Testing of wool-keratin binding.

Main Results:

Keratin exhibited reduced lysyl amine content post-mTGase treatment, indicating self-crosslinking.
Gel electrophoresis showed increased protein band molecular weights, confirming crosslinking.
FTIR spectra revealed an increased amide II band, supporting transamidation.
The mTGase-keratin system effectively bound wool to wool, keratin to wool, and keratin to keratin.

Conclusions:

Low molecular weight keratin can be effectively self-crosslinked by mTGase.
This enzymatic crosslinking enhances wool fabric strength and dimensional stability.
The developed system offers versatile binding capabilities for keratin and wool materials.