Mechanochemically Induced Controlled Glycation of Lysozyme and Its Effect on Enzymatic Activity and Conformational Changes

Xing, Haoran; Yaylayan, Varoujan A.

doi:10.1021/acs.jafc.9b00070

Cited by 11 publications

(9 citation statements)

References 45 publications

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“…Lysozyme can be protected by polyols and sugars versus heat, because they affected hydrophobic interactions ( 44 ). Xing and Yaylayan stated that the presence of sugars could even maintain the enzymatic activity of lysozyme after milling ( 48 ). The most important factors that affect the catalytic rate of lysozyme are shown in Figure 2 .…”

Section: Antimicrobial Activity Of Lysozymementioning

confidence: 99%

An Overview of Antimicrobial Activity of Lysozyme and Its Functionality in Cheese

et al. 2022

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Due to the concern of consumers about the presence of synthetic preservatives, researchers and food manufacturers have recently conducted extensive research on the limited use of these preservatives and the introduction and use of natural preservatives, such as herbal extracts and essential oils, bacteriocins, and antimicrobial enzymes. Lysozyme is a natural enzyme with antimicrobial activity that has attracted considerable attention to be potentially utilized in various industries. Since lysozyme is an intrinsic component of the human immune system and has low toxicity; it could be considered as a natural antimicrobial agent for use in food and pharmaceutical industries. Lysozyme exerts antimicrobial activity against microorganisms, especially Gram-positive bacteria, by hydrolyzing 1,4-beta-linkages between N-acetylmuramic acid and N-acetylglucosamine in the cell wall. In addition, increased antimicrobial activity of lysozyme against Gram-negative bacteria could be achieved by the modification of lysozyme through physical or chemical interactions. Lysozyme is presented as a natural preservative in mammalian milk and can be utilized as a bio-preservative in dairy products, such as cheese. Both bacteria and fungi can contaminate and spoil the cheese; especially the one that is made traditionally by raw milk. Furthermore, uncontrolled and improper processes and post-pasteurization contamination can participate in the cheese contamination. Therefore, besides common preservative strategies applied in cheese production, lysozyme could be utilized alone or in combination with other preservative strategies to improve the safety of cheese. Hence, this study aimed to review the antimicrobial properties of lysozyme as natural antimicrobial enzyme and its functionality in cheese.

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Section: Antimicrobial Activity Of Lysozymementioning

confidence: 99%

An Overview of Antimicrobial Activity of Lysozyme and Its Functionality in Cheese

et al. 2022

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“…Lysozyme is a protein consisting of ~40% of the α-helical structure and has six lysine residues and eleven arginine residues as potential glycation sites [84,85]. Studies previously showed that glycation alters conformation of lysozyme secondary and tertiary structures, and the loss of α-helix results in reduction in its bactericidal and enzymatic activity, thereby increasing susceptibility to bacterial infections in diabetes [86][87][88].…”

Section: Plos Onementioning

confidence: 99%

Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme

et al. 2022

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Glycation process refers to reactions between reduction sugars and amino acids that can lead to formation of advanced glycation end products (AGEs) which are related to changes in chemical and functional properties of biological structures that accumulate during aging and diseases. The aim of this study was to perform and analyze in vitro glycation by fructose and methylglyoxal (MGO) using salivary fluid, albumin, lysozyme, and salivary α-amylase (sAA). Glycation effect was analyzed by biochemical and spectroscopic methods. The results were obtained by fluorescence analysis, infrared spectroscopy (total attenuated reflection—Fourier transform, ATR-FTIR) followed by multivariate analysis of principal components (PCA), protein profile, immunodetection, enzymatic activity and oxidative damage to proteins. Fluorescence increased in all glycated samples, except in saliva with fructose. The ATR-FTIR spectra and PCA analysis showed structural changes related to the vibrational mode of glycation of albumin, lysozyme, and salivary proteins. Glycation increased the relative molecular mass (Mr) in protein profile of albumin and lysozyme. Saliva showed a decrease in band intensity when glycated. The analysis of sAA immunoblotting indicated a relative reduction in intensity of its correspondent Mr after sAA glycation; and a decrease in its enzymatic activity was observed. Carbonylation levels increased in all glycated samples, except for saliva with fructose. Thiol content decreased only for glycated lysozyme and saliva with MGO. Therefore, glycation of salivary fluid and sAA may have the potential to identify products derived by glycation process. This opens perspectives for further studies on the use of saliva, an easy and non-invasive collection fluid, to monitor glycated proteins in the aging process and evolution of diseases.

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“…The most probable assignments of molecular vibrations at the 12 wavenumber positions are as follows: − 1338 cm –1 (the ring vibration of tryptophan), 1404 cm –1 (the symmetric COO – vibrations of aspartate and glutamate side chains), 1454 cm –1 (the amide II′ mode), 1514 cm –1 (the ring vibration of tyrosine), 1545 cm –1 (the amide II mode for β-sheet), 1549 cm –1 (the amide II mode), 1560 cm –1 (the amide II mode for α-helix), , 1583 cm –1 (the asymmetric COO – vibrations of aspartate and glutamate side chains), 1609 cm –1 (the ring vibration of tyrosine and the CN 3 H 5 + side-chain vibration of arginine), 1630 cm –1 (the amide I′ mode), 1651 cm –1 (the amide I mode), and 1686 cm –1 (the amide I mode for β-turn). , Please note that the band assignment to a wavenumber position does not perfectly correspond to the molecular vibration of a small group of a lysozyme molecule because of the overlapping of bands. But when a band overlapping is not too large and the band is situated more separately, one may discuss the sequential order of the physical/chemical “events” of small groups of a lysozyme molecule.…”

Section: Application To the Infrared Spectra Of An H–d Exchange Proce...mentioning

confidence: 99%

Automatic Determination of the Sequential Order of Dynamic Data and Its Application to Vibrational Spectroscopy

Miyata

Nakabayashi

Morita

2020

J. Chem. Inf. Model.

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For over the past 30 years, generalized two-dimensional correlation spectroscopy has formed an active and widespread research area. One of the most attractive properties of this method is that one can determine the sequential order of signal changes. But the determination of the sequential order has only been done manually for several arbitrarily chosen bands. In this paper, we develop a method to automatically determine the sequential order of all of the band intensity changes, and we applied this method to band changes of vibration spectra. This method will open a door to analyze more complicated signals often seen in life phenomena.

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Mechanochemically Induced Controlled Glycation of Lysozyme and Its Effect on Enzymatic Activity and Conformational Changes

Cited by 11 publications

References 45 publications

An Overview of Antimicrobial Activity of Lysozyme and Its Functionality in Cheese

An Overview of Antimicrobial Activity of Lysozyme and Its Functionality in Cheese

Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme

Automatic Determination of the Sequential Order of Dynamic Data and Its Application to Vibrational Spectroscopy

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