Many proteins contain free sulfhydryl groups which can be involved in a variety of biochemical reactions. Reactive thiol groups can either reside within the active center of oxidoreductases or represent a part of a thiol-based redox switch in proteins. Therefore, the exact position of a free sulfhydryl within a protein is mostly very important.This chapter describes a mass spectrometry-based method to determine the location of protein sulfhydryl groups exemplary shown for a synthetic decapeptide and the plasma glycoprotein von Willebrand factor (VWF). We outline (1) labeling of free sulfhydryl groups, (2) enrichment of labeled peptides, and (3) detection and identification of labeled peptides by mass spectrometry.
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http://dx.doi.org/10.1007/978-1-4939-9055-9_12 | DOI Listing |
J Sci Food Agric
January 2025
College of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, China.
Background: The quality of Acipenser sinensis deteriorates significantly during frozen storage due to its high water, protein, and unsaturated fatty acid content. Conventional freezing methods are insufficient to preserve it effectively. This study investigated the effects of liquid nitrogen freezing (LNF) on the quality and myofibrillar protein (MP) characteristics of A.
View Article and Find Full Text PDFJ Food Sci
January 2025
Department of Food Science, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Protein bar hardening negatively impacts shelf life, quality, and consumer acceptance. Although oxidation is known to negatively affect the flavor and texture of foods, the specific roles of lipid and protein oxidation in bar hardening have not been thoroughly investigated. Furthermore, most research has concentrated on dairy proteins, with a notable lack of studies addressing the hardening of plant-based protein bars.
View Article and Find Full Text PDFJ Sci Food Agric
January 2025
Division of Medicine, University College London, London, UK.
Background: The escalating global prevalence of food allergies has intensified the need for hypoallergenic food products. Transglutaminase (TGase)-mediated crosslinking has garnered significant attention for its potential to reduce the allergenicity of food proteins. This study aimed to investigate the effects of TGase crosslinking on the potential allergenicity and conformational changes in a dual-protein system composed of β-lactoglobulin (β-LG) and soy protein isolate (SPI) at varying mass ratios (10:0, 7:3, 5:5, 3:7 and 0:10 (w/w)).
View Article and Find Full Text PDFJ Sci Food Agric
January 2025
College of Food Science and Technology, Bohai University, Jinzhou, China.
Background: Soy protein isolate (SPI) has poor emulsifying ability because of its low molecular flexibility and compact structure, limiting its application in extruded protein-based foods. Extrusion technology has emerged as a promising way to alter the structural properties of proteins. Therefore, the impacts of grape seed proanthocyanidin (GSP) on structural and emulsifying characteristics of SPI in extrusion field were explored in this study.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
School of Food science and Engineering, Shaanxi University of Science and Technology, Xi'an 710021, China; School of Biological and Pharmaceutical Sciences, Shaanxi University of Science and Technology, Xi'an 710021, China; Xi' an Key Laboratory of Precision Nutrition and Functional Product Innovation, Shaanxi University of Science and Technology, Xi'an 710021, China. Electronic address:
This study investigates the effects of ultrasound synergistic pH shift modification on the structural and functional properties of Hericium erinaceus (HE) proteins. The modification resulted in significant changes in the molecular structure of HE proteins, including increased solubility (49.69 % at pH 1.
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