Related Experiment Video
Updated: Dec 25, 2025

NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements
Published on: May 1, 2017
Effect of Different Cooking Methods on Proton Dynamics and Physicochemical Attributes in Spanish Mackerel Assessed by
Shan Sun1,2,3,4, Siqi Wang1,2,3,4, Rong Lin1,2,3,4
1School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, Liaoning, China.
Abstract:
The states of protons within food items are highly related to their physical attributes. In this study, the effect of cooking methods including boiling, steaming, roasting and frying on proton dynamics, physicochemical parameters and microstructure of Spanish mackerel was assessed by low-field nuclear magnetic resonance (LF-NMR) and magnetic resonance imaging (MRI) techniques. The treatment of cooking resulted in a significant reduction of proton mobility and declined freedom of protons. The state changes of protons can be monitored easily in an intuitive and non-destructive manner during various cooking process. The treatments of boiling, steaming, roasting and frying resulted in different cooking loss and similar water-holding capability. A significant increase of total carbonyl content and thiobarbituric acid reactive substances was found, while a decrease of the values for free thiols and surface hydrophobicity was observed. The analysis of circular dichroism spectroscopy and cryo-scanning electron microscopy showed significant structural change. The correlation coefficients of Rcal2 and Rcv2 from partial least squares (PLS) regression models were more than 0.980, suggesting good correlation between LF-NMR data and hardness, resilience, springiness, chewiness, gumminess, and adhesiveness. Good recoveries and a relatively small coefficient of variation (CV) were obtained from the PLS regression models, indicating good reliability and accuracy in predicting texture parameters for mackerel samples.
More Related Videos
10:28Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
Published on: November 2, 2018
09:25Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
Related Concept Videos
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
Proton (¹H) NMR: Chemical Shift
Absorption signals of all the protium nuclei...
Applications Of NMR In Biology
NMR Spectroscopy: Spin–Spin Coupling
Double Resonance Techniques: Overview
Spin decoupling is usually achieved by...
Proteomics
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...