ArticleScientific reports2020
Fourier-transform infrared spectroscopy for monitoring proteolytic reactions using dry-films treated with trifluoroacetic acid.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
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- A Solution-Based Deposition Method Enabling Pigment Blue Edible Electrochemical Transistors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Preparation, characterization, antioxidant activity evaluation, and potential application of Peruvian squid liver protein hydrolysates.Food chemistry: X · 2025Article
- Silk Sericin-Based Electrospun Nanofibers Forming Films for Cosmetic Applications: Preparation, Characterization, and Efficacy Evaluation.Molecules (Basel, Switzerland) · 2025Article
- Article
- Cross-Linked Enzyme Aggregate (CLEA) Preparation from Waste Activated Sludge.Microorganisms · 2023Article
- Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study we explore the potential of using Fourier-transform infrared (FTIR) spectra of trifluoroacetate-protein and peptide complexes for monitoring proteolytic reactions. The idea of treating dry-films of protein hydrolysates with trifluoroacetic acid (TFA) prior to FTIR analysis is based on the unique properties of TFA. By adding a large excess of TFA to protein hydrolysate samples, the possible protonation sites of the proteins and peptides will be saturated. In addition, TFA has a low boiling point when protonated as well as complex-forming abilities. When forming TFA-treated dry-films of protein hydrolysates, the excess TFA will evaporate and the deprotonated acid (CF
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