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Updated: Nov 19, 2025

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

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Published on: May 25, 2018

Deviation of Trypsin Activity Using Peptide Conformational Imprints.

Kiran Reddy Kanubaddi¹, Pei-Yu Huang², Ya-Lin Chang²

¹Department of Life Science, National Dong Hwa University, Hualien 97401, Taiwan.

Nanomaterials (Basel, Switzerland)

|January 30, 2021

Summary

Peptide conformational imprints (PCIs) were used to immobilize porcine pancreatic alpha-trypsin (PPT) on magnetic particles. This method sustained enzyme activity and stability over multiple cycles, demonstrating effective enzyme immobilization.

Keywords:

conformational imprint magnetic particles molecularly-imprinted polymers porcine pancreatic trypsin secondary structure

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Published on: May 13, 2020

Area of Science:

Biochemistry
Enzyme immobilization
Materials Science

Background:

Enzyme immobilization is crucial for biocatalysis and enzyme reusability.
Developing specific and stable immobilization methods remains a challenge.
Porcine pancreatic alpha-trypsin (PPT) is a widely studied enzyme with significant biotechnological applications.

Purpose of the Study:

To develop a novel methodology for site-specific immobilization of porcine pancreatic alpha-trypsin (PPT).
To utilize peptide conformational imprints (PCIs) on magnetic particles (PCIMPs) for targeted enzyme capture.
To evaluate the catalytic activity, kinetic parameters, and stability of immobilized PPT.

Main Methods:

Fabrication of segment-mediated PCIs on magnetic particles (PCIMPs) to create cavities complementary to PPT structure.
Immobilization of PPT using template-derived PCIMPs based on specific PPT sequences.
Assessment of hydrolytic activity using N-benzoyl-L-arginine ethyl ester (BAEE) and high-performance liquid chromatography (HPLC).
Kinetic analysis using Lineweaver-Burk plots to determine inhibition type and kinetic parameters.

Main Results:

PCIMPs successfully created specific cavities for PPT immobilization.
The immobilized PPT exhibited non-competitive inhibition towards the substrate BAEE.
Optimized kinetic parameters for PPT/PCIMPs 233-245+G were determined (V = 1.47 × 10^-3 mM s^-1, K = 0.42 mM, k = 1.16 s^-1, k/K = 2.79 mM^-1 s^-1).
Immobilized PPT maintained stable catalytic activity over four successive cycles.

Conclusions:

Peptide conformational imprints provide an effective strategy for site-specific enzyme immobilization.
The PCIMP method enhances the stability and reusability of porcine pancreatic alpha-trypsin.
This approach offers a promising platform for developing robust biocatalytic systems.