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包裹于非离子表面活性剂泡囊和明胶膜中的噬菌体裂解蛋白CHAPSH3b

Phage Lytic Protein CHAPSH3b Encapsulated in Niosomes and Gelatine Films.

作者信息

Marchianò Verdiana, Duarte Ana Catarina, Agún Seila, Luque Susana, Marcet Ismael, Fernández Lucía, Matos María, Blanco Mª Del Carmen, García Pilar, Gutiérrez Gemma

机构信息

Department of Physical and Analytical Chemistry, University of Oviedo, Julián Clavería 8, 33006 Oviedo, Spain.

Department of Chemical and Environmental Engineering, University of Oviedo, Julián Clavería 8, 33006 Oviedo, Spain.

出版信息

Microorganisms. 2024 Jan 6;12(1):119. doi: 10.3390/microorganisms12010119.

DOI:10.3390/microorganisms12010119
PMID:38257944
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10819965/
Abstract

Antimicrobial resistance (AMR) has emerged as a global health challenge, sparking worldwide interest in exploring the antimicrobial potential of natural compounds as an alternative to conventional antibiotics. In recent years, one area of focus has been the utilization of bacteriophages and their derivative proteins. Specifically, phage lytic proteins, or endolysins, are specialized enzymes that induce bacterial cell lysis and can be efficiently produced and purified following overexpression in bacteria. Nonetheless, a significant limitation of these proteins is their vulnerability to certain environmental conditions, which may impair their effectiveness. Encapsulating endolysins in vesicles could mitigate this issue by providing added protection to the proteins, enabling controlled release, and enhancing their stability, particularly at temperatures around 4 °C. In this work, the chimeric lytic protein CHAPSH3b was encapsulated within non-ionic surfactant-based vesicles (niosomes) created using the thin film hydrating method (TFH). These protein-loaded niosomes were then characterized, revealing sizes in the range of 30-80 nm, zeta potentials between 30 and 50 mV, and an encapsulation efficiency (EE) of 50-60%. Additionally, with the objective of exploring their potential application in the food industry, these endolysin-loaded niosomes were incorporated into gelatine films. This was carried out to evaluate their stability and antimicrobial efficacy against .

摘要

抗菌耐药性(AMR)已成为一项全球卫生挑战,引发了全球对探索天然化合物抗菌潜力以替代传统抗生素的兴趣。近年来,一个关注领域是噬菌体及其衍生蛋白的利用。具体而言,噬菌体裂解蛋白,即内溶素,是诱导细菌细胞裂解的特殊酶,在细菌中过表达后可高效生产和纯化。然而,这些蛋白的一个重大局限是它们易受某些环境条件影响,这可能损害其有效性。将内溶素包裹在囊泡中可以通过为蛋白提供额外保护、实现控释并增强其稳定性(特别是在4℃左右的温度下)来缓解这一问题。在这项工作中,嵌合裂解蛋白CHAPSH3b被包裹在使用薄膜水化法(TFH)制备的基于非离子表面活性剂的囊泡(脂质体)中。然后对这些负载蛋白的脂质体进行了表征,结果显示其尺寸在30 - 80nm范围内,zeta电位在30至50mV之间,包封率(EE)为50 - 60%。此外,为了探索它们在食品工业中的潜在应用,将这些负载内溶素的脂质体掺入明胶薄膜中。这样做是为了评估它们对……的稳定性和抗菌效果。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/2f61dbf4bc15/microorganisms-12-00119-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/ff518f206273/microorganisms-12-00119-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/109245062d12/microorganisms-12-00119-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/51bf96779f09/microorganisms-12-00119-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/4c107ad82775/microorganisms-12-00119-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/e798b17cae84/microorganisms-12-00119-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/52290687b85f/microorganisms-12-00119-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/2f61dbf4bc15/microorganisms-12-00119-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/ff518f206273/microorganisms-12-00119-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/109245062d12/microorganisms-12-00119-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/51bf96779f09/microorganisms-12-00119-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/4c107ad82775/microorganisms-12-00119-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/e798b17cae84/microorganisms-12-00119-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/52290687b85f/microorganisms-12-00119-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e31/10819965/2f61dbf4bc15/microorganisms-12-00119-g007.jpg

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