NDLI: Monitoring of Demasking of Peptide Bonds During Proteolysis by Analysis of the Apparent Spectral Shift of Intrinsic Protein Fluorescence

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Monitoring of Demasking of Peptide Bonds During Proteolysis by Analysis of the Apparent Spectral Shift of Intrinsic Protein Fluorescence

Content Provider	Springer Nature Link
Author	Vorob’ev, Mikhail M. Vogel, Vitali Güler, Günnur Mäntele, Werner
Copyright Year	2011
Abstract	Demasking of peptide bonds during proteolysis of β-casein and β-lactoglobulin by trypsin was monitored by the measurement of the overall spectral shift of intrinsic protein fluorescence. A clear shift of the apparent emission maxima from approximately 340–345 nm to 355–360 nm during proteolysis was observed, with a time course, which follows protein degradation and structural opening. In contrast to procedures using extrinsic fluorescence labels, this label-free procedure does not bear the risk of structural alterations. It is easy to perform, fast, and has a relatively high accuracy of determination. Proteolysis was modelled as simple two-step process with consecutive demasking and hydrolysis stages. It was shown that the fluorescence shift can be attributed to the demasking stage. Formally, kinetics of the peptide bond demasking obeys a first-order kinetic law. Both the theoretical simulations and experiment are in accordance giving the similar dependences of the hydrolysis degree on the degree of peptide bond demasking.
Starting Page	519
Ending Page	526
Page Count	8
File Format	PDF
ISSN	15571858
Journal	Food Biophysics
Volume Number	6
Issue Number	4
e-ISSN	15571866
Language	English
Publisher	Springer US
Publisher Date	2011-08-12
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Tryptophan fluorescence Tryptic digestion β-casein β-lactoglobulin Proteolysis kinetics Peptide bond demasking Biophysics and Biological Physics Analytical Chemistry Food Science
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Biophysics Bioengineering Food Science Applied Microbiology and Biotechnology

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Demasking of Peptide Bonds During Tryptic Hydrolysis of β-casein in the Presence of Ethanol

Tryptophan Fluorescence and Time-lag Hydrolysis of Peptide Bonds during Degradation of β-lactoglobulin by Trypsin

Proteolysis of β-lactoglobulin by Trypsin: Simulation by Two-Step Model and Experimental Verification by Intrinsic Tryptophan Fluorescence

Kinetic modeling of demasking and hydrolysis of peptide bonds during proteolysis of ß-lactoglobulin by trypsin.

Modeling of Proteolysis of β-Lactoglobulin and β-Casein by Trypsin with Consideration of Secondary Masking of Intermediate Polypeptides

Kinetic modeling of demasking and hydrolysis of peptide bonds during proteolysis of β-lactoglobulin by trypsin

Interaction of β-Lactoglobulin with Small Hydrophobic Ligands - Influence of Covalent AITC Modification on β-LG Tryptic Cleavage

Enzyme-Induced Formation of β-Lactoglobulin Fibrils by AspN Endoproteinase

Influence of mathematical models and correction factors on binding results of polyphenols and retinol with β-lactoglobulin measured with fluorescence quenching

Monitoring of Demasking of Peptide Bonds During Proteolysis by Analysis of the Apparent Spectral Shift of Intrinsic Protein Fluorescence

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Monitoring of Demasking of Peptide Bonds During Proteolysis by Analysis of the Apparent Spectral Shift of Intrinsic Protein Fluorescence