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Lysozyme and Its Application as Antibacterial Agent in Food Industry

Lysozymes are hydrolytic enzymes characterized by their ability to cleave the β-(1,4)-glycosidic bonds in peptidoglycan, a major structural component of the bacterial cell wall. This hydrolysis action compromises the integrity of the cell wall, causing the lysis of bacteria. For more than 80 years,...

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Detalles Bibliográficos
Autores principales: Nawaz, Nida, Wen, Sai, Wang, Fenghuan, Nawaz, Shiza, Raza, Junaid, Iftikhar, Maryam, Usman, Muhammad
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9572377/
https://www.ncbi.nlm.nih.gov/pubmed/36234848
http://dx.doi.org/10.3390/molecules27196305
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author Nawaz, Nida
Wen, Sai
Wang, Fenghuan
Nawaz, Shiza
Raza, Junaid
Iftikhar, Maryam
Usman, Muhammad
author_facet Nawaz, Nida
Wen, Sai
Wang, Fenghuan
Nawaz, Shiza
Raza, Junaid
Iftikhar, Maryam
Usman, Muhammad
author_sort Nawaz, Nida
collection PubMed
description Lysozymes are hydrolytic enzymes characterized by their ability to cleave the β-(1,4)-glycosidic bonds in peptidoglycan, a major structural component of the bacterial cell wall. This hydrolysis action compromises the integrity of the cell wall, causing the lysis of bacteria. For more than 80 years, its role of antibacterial defense in animals has been renowned, and it is also used as a preservative in foods and pharmaceuticals. In order to improve the antimicrobial efficacy of lysozyme, extensive research has been intended for its modifications. This manuscript reviews the natural antibiotic compound lysozyme with reference to its catalytic and non-catalytic mode of antibacterial action, lysozyme types, susceptibility and resistance of bacteria, modification of lysozyme molecules, and its applications in the food industry.
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spelling pubmed-95723772022-10-17 Lysozyme and Its Application as Antibacterial Agent in Food Industry Nawaz, Nida Wen, Sai Wang, Fenghuan Nawaz, Shiza Raza, Junaid Iftikhar, Maryam Usman, Muhammad Molecules Review Lysozymes are hydrolytic enzymes characterized by their ability to cleave the β-(1,4)-glycosidic bonds in peptidoglycan, a major structural component of the bacterial cell wall. This hydrolysis action compromises the integrity of the cell wall, causing the lysis of bacteria. For more than 80 years, its role of antibacterial defense in animals has been renowned, and it is also used as a preservative in foods and pharmaceuticals. In order to improve the antimicrobial efficacy of lysozyme, extensive research has been intended for its modifications. This manuscript reviews the natural antibiotic compound lysozyme with reference to its catalytic and non-catalytic mode of antibacterial action, lysozyme types, susceptibility and resistance of bacteria, modification of lysozyme molecules, and its applications in the food industry. MDPI 2022-09-24 /pmc/articles/PMC9572377/ /pubmed/36234848 http://dx.doi.org/10.3390/molecules27196305 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Nawaz, Nida
Wen, Sai
Wang, Fenghuan
Nawaz, Shiza
Raza, Junaid
Iftikhar, Maryam
Usman, Muhammad
Lysozyme and Its Application as Antibacterial Agent in Food Industry
title Lysozyme and Its Application as Antibacterial Agent in Food Industry
title_full Lysozyme and Its Application as Antibacterial Agent in Food Industry
title_fullStr Lysozyme and Its Application as Antibacterial Agent in Food Industry
title_full_unstemmed Lysozyme and Its Application as Antibacterial Agent in Food Industry
title_short Lysozyme and Its Application as Antibacterial Agent in Food Industry
title_sort lysozyme and its application as antibacterial agent in food industry
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9572377/
https://www.ncbi.nlm.nih.gov/pubmed/36234848
http://dx.doi.org/10.3390/molecules27196305
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