Heat-Treated Lysozyme Hydrochloride: A Study on Its Structural Modifications and Anti-SARS-CoV-2 Activity
Lysozyme (E.C. 3.2.1.17), an about 14 kDa protein and pI 11, widely spread in nature, is present in humans mainly in milk, saliva, and intestinal mucus as a part of innate defense mechanisms. It is endowed with antimicrobial activity due to its action as an N-acetylmuramidase, cleaving the 1-4β glyc...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-03-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/28/6/2848 |
| _version_ | 1827748351021416448 |
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| author | Serena Delbue Elena Pariani Silvia Parapini Cristina Galli Nicoletta Basilico Sarah D’Alessandro Sara Pellegrino Elena Pini Samuele Ciceri Patrizia Ferraboschi Paride Grisenti |
| author_facet | Serena Delbue Elena Pariani Silvia Parapini Cristina Galli Nicoletta Basilico Sarah D’Alessandro Sara Pellegrino Elena Pini Samuele Ciceri Patrizia Ferraboschi Paride Grisenti |
| author_sort | Serena Delbue |
| collection | DOAJ |
| description | Lysozyme (E.C. 3.2.1.17), an about 14 kDa protein and pI 11, widely spread in nature, is present in humans mainly in milk, saliva, and intestinal mucus as a part of innate defense mechanisms. It is endowed with antimicrobial activity due to its action as an N-acetylmuramidase, cleaving the 1-4β glycosidic linkage in the peptidoglycan layer of Gram-positive bacteria. This antimicrobial activity is exerted only against a limited number of Gram-negative bacteria. Different action mechanisms are proposed to explain its activity against Gram-negative bacteria, viruses, and fungi. The antiviral activity prompted the study of a possible application of lysozyme in the treatment of SARS-CoV-2 infections. Among the different sources of lysozyme, the chicken egg albumen was chosen, being the richest source of this protein (c-type lysozyme, 129 amino acids). Interestingly, the activity of lysozyme hydrochloride against SARS-CoV-2 was related to the heating (to about 100 °C) of this molecule. A chemical–physical characterization was required to investigate the possible modifications of native lysozyme hydrochloride by heat treatment. The FTIR analysis of the two preparations of lysozyme hydrochloride showed appreciable differences in the secondary structure of the two protein chains. HPLC and NMR analyses, as well as the enzymatic activity determination, did not show significant modifications. |
| first_indexed | 2024-03-11T06:06:04Z |
| format | Article |
| id | doaj.art-4f92bd36551a4faf955ec76a98c077f9 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-11T06:06:04Z |
| publishDate | 2023-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-4f92bd36551a4faf955ec76a98c077f92023-11-17T12:56:02ZengMDPI AGMolecules1420-30492023-03-01286284810.3390/molecules28062848Heat-Treated Lysozyme Hydrochloride: A Study on Its Structural Modifications and Anti-SARS-CoV-2 ActivitySerena Delbue0Elena Pariani1Silvia Parapini2Cristina Galli3Nicoletta Basilico4Sarah D’Alessandro5Sara Pellegrino6Elena Pini7Samuele Ciceri8Patrizia Ferraboschi9Paride Grisenti10Department of Biomedical, Surgical and Dental Sciences, Università degli Studi di Milano, 20133 Milan, ItalyDepartment of Biomedical Sciences for Health, Università degli Studi di Milano, 20133 Milan, ItalyDepartment of Biomedical Sciences for Health, Università degli Studi di Milano, 20133 Milan, ItalyDepartment of Biomedical Sciences for Health, Università degli Studi di Milano, 20133 Milan, ItalyDepartment of Biomedical, Surgical and Dental Sciences, Università degli Studi di Milano, 20133 Milan, ItalyDepartment of Pharmacological and Biomedical Sciences, Università degli Studi di Milano, 20133 Milan, ItalyDepartment of Pharmaceutical Sciences, General and Organic Chemistry Section “Alessandro Marchesini”, University of Milan, 20133 Milan, ItalyDepartment of Pharmaceutical Sciences, General and Organic Chemistry Section “Alessandro Marchesini”, University of Milan, 20133 Milan, ItalyDepartment of Pharmaceutical Sciences, University of Milan, Via L. Mangiagalli 25, 20133 Milan, ItalyDepartment of Medical Biotechnology and Translational Medicine, Università degli Studi di Milano, Via Saldini 50, 20133 Milan, ItalyBioseutica, Landbouwweg 83, 3899 BD Zeewolde, The NetherlandsLysozyme (E.C. 3.2.1.17), an about 14 kDa protein and pI 11, widely spread in nature, is present in humans mainly in milk, saliva, and intestinal mucus as a part of innate defense mechanisms. It is endowed with antimicrobial activity due to its action as an N-acetylmuramidase, cleaving the 1-4β glycosidic linkage in the peptidoglycan layer of Gram-positive bacteria. This antimicrobial activity is exerted only against a limited number of Gram-negative bacteria. Different action mechanisms are proposed to explain its activity against Gram-negative bacteria, viruses, and fungi. The antiviral activity prompted the study of a possible application of lysozyme in the treatment of SARS-CoV-2 infections. Among the different sources of lysozyme, the chicken egg albumen was chosen, being the richest source of this protein (c-type lysozyme, 129 amino acids). Interestingly, the activity of lysozyme hydrochloride against SARS-CoV-2 was related to the heating (to about 100 °C) of this molecule. A chemical–physical characterization was required to investigate the possible modifications of native lysozyme hydrochloride by heat treatment. The FTIR analysis of the two preparations of lysozyme hydrochloride showed appreciable differences in the secondary structure of the two protein chains. HPLC and NMR analyses, as well as the enzymatic activity determination, did not show significant modifications.https://www.mdpi.com/1420-3049/28/6/2848peptidoglycan-degrading enzymeinnate immunityantibiotic activityantiviral activityNMRFTIR |
| spellingShingle | Serena Delbue Elena Pariani Silvia Parapini Cristina Galli Nicoletta Basilico Sarah D’Alessandro Sara Pellegrino Elena Pini Samuele Ciceri Patrizia Ferraboschi Paride Grisenti Heat-Treated Lysozyme Hydrochloride: A Study on Its Structural Modifications and Anti-SARS-CoV-2 Activity Molecules peptidoglycan-degrading enzyme innate immunity antibiotic activity antiviral activity NMR FTIR |
| title | Heat-Treated Lysozyme Hydrochloride: A Study on Its Structural Modifications and Anti-SARS-CoV-2 Activity |
| title_full | Heat-Treated Lysozyme Hydrochloride: A Study on Its Structural Modifications and Anti-SARS-CoV-2 Activity |
| title_fullStr | Heat-Treated Lysozyme Hydrochloride: A Study on Its Structural Modifications and Anti-SARS-CoV-2 Activity |
| title_full_unstemmed | Heat-Treated Lysozyme Hydrochloride: A Study on Its Structural Modifications and Anti-SARS-CoV-2 Activity |
| title_short | Heat-Treated Lysozyme Hydrochloride: A Study on Its Structural Modifications and Anti-SARS-CoV-2 Activity |
| title_sort | heat treated lysozyme hydrochloride a study on its structural modifications and anti sars cov 2 activity |
| topic | peptidoglycan-degrading enzyme innate immunity antibiotic activity antiviral activity NMR FTIR |
| url | https://www.mdpi.com/1420-3049/28/6/2848 |
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