Predicting hydrolysis of whey protein by mid-infrared spectroscopy

Poulsen, Nina Aagaard; Eskildsen, Carl Emil; Akkerman, Marije; Johansen, Lene Buhelt; Hansen, Mikka Stenholdt; Hansen, Per Waaben; Skov, Thomas; Larsen, Lotte Bach

doi:10.1016/j.idairyj.2016.04.002

Cited by 50 publications

(21 citation statements)

References 22 publications

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“…An alternative to the degree of hydrolysis could be the degree of changes in a secondary structure and the conformation of protein substrate, as measured by an appropriate spectral technique. In recent years, some progress has been made in comparing spectral data obtained at different times of hydrolysis using fluorescence [12,13] and infrared spectroscopies [14][15][16][17]. It was demonstrated that the degradation of protein substrate can be quantified by a shift in tryptophan fluorescence [12,13].…”

Section: Introductionmentioning

confidence: 99%

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

Vorob’ev

2019

Symmetry

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To distinguish differences in enzymatic hydrolysis of various proteins, we propose an algorithm using a dataset of fluorescence spectra obtained at different moments of hydrolysis t. This algorithm was demonstrated in the example of β-lactoglobulin (β-LG) proteolysis by trypsin. The procedure involved processing the spectra to obtain the wavelength of the maximum fluorescence λmax, which was found to be proportional to the fraction of tryptophanes in hydrated proteolysis products (demasked tryptophanes). Then, the dependence λmax(t) was fitted by biexponential function with two exponential terms, one of which was responsible for the fast part of the fluorescence change during proteolysis. The contribution of this term was quite different for various protein substrates—it was positive for β-LG and negative for β-casein. The observed differences in proteolysis of different substrates were explained by different demasking processes. Combining the fluorescence data with the degrees of hydrolysis of peptide bonds allowed us to analyze the hydrolysis of β-LG in the framework of the two-step proteolysis model and estimate the ratio of rate constants of demasking and hydrolysis and the percentages of initially masked and resistant peptide bonds. This model predicted the existence of a bimodal demasking process with a fast part at the beginning of proteolysis and lag-type kinetics of release for some peptides. Compared with monitoring proteolysis in terms of the degree of hydrolysis only, the fluorescence data are helpful for the recognition of proteolysis patterns.

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Section: Introductionmentioning

confidence: 99%

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

Vorob’ev

2019

Symmetry

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“…This limits their use in industrial settings and as potential online monitoring tools. Recently, it has been shown that Fourier Transform Infrared Spectroscopy (FTIR) spectra are useful for characterization of enzymatic protein hydrolysates [51][52]. This technique holds a promising potential as an on-or at-line process monitoring tool for measurements of degree of hydrolysis.…”

Section: Discussionmentioning

confidence: 99%

Valorization of Proteins from Co- and By-Products from the Fish and Meat Industry

et al. 2017

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“…The observed changes in the FTOR of zein, zein hydrolysate and the glycosylated hydrolysate are shown in Figure 2A. The band around 1400 cm -1 is assigned as the symmetric stretch in CDDfunctional groups (Poulsen et al, 2016), while the band at 1516 cm -1 is attributed to the -NH 3+ scissoring vibrational mode (Perros et al, 2013). The intensity of bands at 1400 cm -1 and 1516 cm -1 of zein hydrolysate was higher than that of zein, indicating the breakdown of amide backbone and formation of amino and carboxylate terminals.…”

Section: Characteristics Of the Glycosylated Hydrolysatementioning

confidence: 98%

Preparation of glycosylated hydrolysate by liquid fermentation with Cordyceps militaris and characterization of its functional properties

Yang¹,

Zheng²,

Li³

et al. 2020

Food Sci. Technol

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This study aimed to investigate the potential of a novel preparation strategy for glycosylated hydrolysate by liquid fermentation in order to provide a high-quality glycosylated hydrolysate. Protein solubility, surface hydrophobicity and antioxidant activity were evaluated. The results of Fourier transform infrared spectra demonstrated the occurrence of glycosylation reaction. The results of Fluorescence emission spectroscope revealed the decrease of tertiary conformation stability. Circular dichroism spectra revealed significant decrease in α-helix and increase in β-sheet and random coil by glycosylation reaction. On comparison with zein hydrolysate, glycosylated hydrolysate had lower surface hydrophobicity but higher in solubility and in vitro digestibility due to glycosylation. Glycosylated hydrolysate presented higher ABTS (2,2'-Azinobis [3-ethylbenzothiazoline-6-sulfonic acid]-diammonium salt) and superoxide radicals scavenging activities as well as Cu 2+ chelating capacity. Ot is concluded that the glycosylation confer an open structure and modified properties of zein, and glycosylated hydrolysate is a potential ingredient with better hydration and antioxidant activities than zein hydrolysate.

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Predicting hydrolysis of whey protein by mid-infrared spectroscopy

Cited by 50 publications

References 22 publications

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

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

Valorization of Proteins from Co- and By-Products from the Fish and Meat Industry

Preparation of glycosylated hydrolysate by liquid fermentation with Cordyceps militaris and characterization of its functional properties

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