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Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...

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Updated: Sep 8, 2025

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Published on: April 6, 2016

Micro-immobilized enzyme reactors for mass spectrometry proteomics.

Zhongjie Yao¹, Yilan Li², Wei Xu¹

¹School of Medical Technology, Beijing Institute of Technology, Beijing 100081, China. weixu@bit.edu.cn.

|June 26, 2025

Summary

Micro-immobilized enzyme reactors (μ-IMERs) enhance enzyme stability and efficiency over traditional methods. This review assesses recent advances in μ-IMER design, fabrication, and proteomic applications for improved workflows.

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Last Updated: Sep 8, 2025

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

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Published on: April 6, 2016

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Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

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Published on: August 17, 2015

Area of Science:

Biochemistry and Analytical Chemistry
Biotechnology and Bioengineering

Background:

Traditional enzymatic methods face limitations in stability and efficiency.
Micro-immobilized enzyme reactors (μ-IMERs) offer significant advantages, including enhanced enzyme stability, reduced reagent consumption, and increased reaction efficiency.
μ-IMERs are crucial for advancing proteomic sample preparation and analytical workflows.

Purpose of the Study:

To review and assess recent advancements in micro-immobilized enzyme reactor (μ-IMER) technology.
To discuss various immobilization methods, μ-IMER designs, and their applications in proteomics.
To summarize the current development status, challenges, and future prospects of μ-IMERs.

Main Methods:

Discussion of common enzyme immobilization techniques: adsorption, covalent binding, affinity binding, and entrapment.
Analysis of different μ-IMER designs: open-tube, packed, monolithic reactors, and membrane-immobilized enzymes.
Presentation of μ-IMER applications in proteomics, focusing on sample preparation and analytical workflows.

Main Results:

Immobilization methods vary in advantages, challenges, and future potential.
Different μ-IMER designs exhibit distinct structural architectures and operational performance characteristics.
μ-IMERs demonstrate significant potential for improving proteomic sample preparation and analytical workflows.

Conclusions:

μ-IMERs represent a superior alternative to traditional enzymatic methods in various applications.
Continued research into μ-IMER design and fabrication will further enhance their utility in proteomics.
Addressing current challenges will unlock new opportunities and drive future innovation in μ-IMER technology.