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新型固定在纤维素纳米纤维上的糜蛋白酶的抗生物膜活性增强和长效作用。

Improved anti-biofilm activity and long-lasting effects of novel serratiopeptidase immobilized on cellulose nanofibers.

机构信息

Department of Tissue Engineering and Applied Cell Science, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.

Nano-Biotechnology Department, New Technologies Research Group, Pasteur Institute of Iran, Tehran, Iran.

出版信息

Appl Microbiol Biotechnol. 2023 Nov;107(21):6487-6496. doi: 10.1007/s00253-023-12734-7. Epub 2023 Sep 6.

Abstract

Today, enzymatic treatment is a progressive field in combating biofilm producing pathogens. In this regard, serratiopeptidase, a medicinally important metalloprotease, has been recently highlighted as an enzyme with proved anti-biofilm activity. In the present study, in order to increase the long-lasting effects of the enzyme, serratiopeptidase and the novel engineered forms with enhanced anti-biofilm activity were immobilized on the surface of cellulose nanofibers (CNFs) as a natural polymer with eminent properties. For this, recombinant serratiopeptidases including the native and previously designed enzymes were produced, purified and conjugated to the CNF by chemical and physical methods. Immobilization was confirmed using different scanning and microscopic methods. The enzyme activity was assessed using casein hydrolysis test. Enzyme release analysis was performed using dialysis tube method. Anti-biofilm activity of free and immobilized enzymes has been examined on Staphylococcus aureus and Pseudomonas aeruginosa strains. Finally, cytotoxicity of enzyme-conjugated CNFs was performed by MTT assay. The casein hydrolysis results confirmed fixation of all recombinant enzymes on CNFs by chemical method; however, inadequate fixation of these enzymes was found using cold atmospheric plasma (CAP). The AFM, FTIR, and SEM analysis confirmed appropriate conjugation of enzymes on the surface of CNFs. Immobilization of enzymes on CNFs improved the anti-biofilm activity of serratiopeptidase enzymes. Interestingly, the novel engineered serratiopeptidase (T344 [8-339ss]) exhibited the highest anti-biofilm activity in both conjugated and non-conjugated forms. In conclusion, incorporation of serratiopeptidases into CNFs improves their anti-biofilm activities without baring any cytotoxicity. KEY POINTS: • Enzymes were successfully immobilized on cellulose nanofibers using chemical method. • Immobilization of enzymes on CNFs improved their anti-biofilm activity. • T344 [8-339ss] exhibited the highest anti-biofilm activity in both conjugated and non-conjugated forms.

摘要

如今,酶处理是对抗产生生物膜的病原体的一个不断发展的领域。在这方面,糜蛋白酶,一种具有重要医学意义的金属蛋白酶,最近被强调为一种具有抗生物膜活性的酶。在本研究中,为了提高酶的长效作用,将糜蛋白酶和具有增强抗生物膜活性的新型工程化形式固定在纤维素纳米纤维(CNF)表面,CNF 是一种具有显著性能的天然聚合物。为此,生产、纯化了包括天然和以前设计的酶的重组糜蛋白酶,并通过化学和物理方法将其与 CNF 偶联。使用不同的扫描和显微镜方法证实了固定化。使用酪蛋白水解试验评估酶活性。通过透析管法进行酶释放分析。研究了游离酶和固定化酶对金黄色葡萄球菌和铜绿假单胞菌的抗生物膜活性。最后,通过 MTT 测定法评估了酶结合 CNF 的细胞毒性。酪蛋白水解结果证实了所有重组酶通过化学方法固定在 CNF 上;然而,通过冷等离体等离子体(CAP)发现这些酶的固定不充分。AFM、FTIR 和 SEM 分析证实了酶在 CNF 表面的适当偶联。酶在 CNF 上的固定化提高了糜蛋白酶酶的抗生物膜活性。有趣的是,新型工程化糜蛋白酶(T344 [8-339ss])在偶联和非偶联形式下均表现出最高的抗生物膜活性。总之,将糜蛋白酶掺入 CNF 可提高其抗生物膜活性而不产生任何细胞毒性。关键点:• 成功地使用化学方法将酶固定在纤维素纳米纤维上。• 酶在 CNF 上的固定化提高了其抗生物膜活性。• T344 [8-339ss] 在偶联和非偶联形式下均表现出最高的抗生物膜活性。

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