ArticleBiology2022
Maximizing Cumulative Trypsin Activity with Calcium at Elevated Temperature for Enhanced Bottom-Up Proteome Analysis.
Article in Biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Mass spectrometry-based proteomics of FFPE tissues: progress, limitations, and clinical translation barriers.Clinical proteomics · 2025Review
- Bovine Serum Albumin-Trypsin Sponges for Enhanced Enzymatic Stability and Protein Digestion Efficiency.ACS applied bio materials · 2025Article
- Proteomic Characterization of 1000 Human and Murine Neutrophils Freshly Isolated From Blood and Sites of Sterile Inflammation.Molecular & cellular proteomics : MCP · 2024Article
- Clean and Complete Protein Digestion with an Autolysis Resistant Trypsin for Peptide Mapping.Journal of proteome research · 2024Article
- Benchmarking and Automating the Biotinylation Proteomics Workflow.Research square · 2024Article
- Proteomic Identification and Label-Free Quantification of Proteins Implicated in Neurite and Spine Formation.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Cheaper, faster, simpler trypsin digestion for high-throughput targeted protein quantification.Journal of mass spectrometry and advances in the clinical lab · 2023Article
- Robust and Easy-to-Use One-Pot Workflow for Label-Free Single-Cell Proteomics.Analytical chemistry · 2023Article
- Stability of enzyme immobilized on the nanofluidic channel surface.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Bottom-up proteomics relies on efficient trypsin digestion ahead of MS analysis. Prior studies have suggested digestion at elevated temperature to accelerate proteolysis, showing an increase in the number of MS-identified peptides. However, improved sequence coverage may be a consequence of partial digestion, as higher temperatures destabilize and degrade the enzyme, causing enhanced activity to be short-lived. Here, we use a spectroscopic (BAEE) assay to quantify calcium-stabilized trypsin activity over the complete time course of a digestion. At 47 °C, the addition of calcium contributes a 25-fold enhancement in trypsin stability. Higher temperatures show a net decrease in cumulative trypsin activity. Through bottom-up MS analysis of a yeast proteome extract, we demonstrate that a 1 h digestion at 47 °C with 10 mM Ca
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Registered trials
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.