L. Daoud, A. H. Brahim, Houda Hmani, A. Akremi, Mouna Jlidi, M. Ali, S. Bejar, Naser Aliye Feto, Mamdouh Ben Ali
{"title":"Salicola sp. strain SBJ9: a novel extremely halophilic bacterium with an interesting protease activity","authors":"L. Daoud, A. H. Brahim, Houda Hmani, A. Akremi, Mouna Jlidi, M. Ali, S. Bejar, Naser Aliye Feto, Mamdouh Ben Ali","doi":"10.3390/mol2net-04-06115","DOIUrl":null,"url":null,"abstract":"A number of newly isolated halophilic microorganisms were screened for protease production. A bacterium designated as strain SBJ9 showed an important enzyme production at high salt concentrations and was then retained. The 16S DNA identification put this strain in the genus of Salicola with two reference species only. Protease production was higher at salinities ranging from 150 to 200 g/l (3.2 M) NaCl, when monitored at 35 °C and pH 7. The protease activity was optimal at 2.5 M NaCl, 40°C and pH 8, with high stability at wide ranges of salinity (1-5 M NaCl), temperatures (2070 °C) and pH values (511). It was slightly improved by 5 mM CaCl2 and totally inhibited by PMSF which indicated the dominance of serine proteases. Besides, it was perfectly stable in the presence of many detergent additives and organic solvents at high concentrations. These important features make Salicola sp. strain SBJ9 protease activity a good candidate for many industrial applications such as detergency and organic synthesis.","PeriodicalId":20475,"journal":{"name":"Proceedings of MOL2NET 2018, International Conference on Multidisciplinary Sciences, 4th edition","volume":"14 3 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2019-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Proceedings of MOL2NET 2018, International Conference on Multidisciplinary Sciences, 4th edition","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3390/mol2net-04-06115","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
A number of newly isolated halophilic microorganisms were screened for protease production. A bacterium designated as strain SBJ9 showed an important enzyme production at high salt concentrations and was then retained. The 16S DNA identification put this strain in the genus of Salicola with two reference species only. Protease production was higher at salinities ranging from 150 to 200 g/l (3.2 M) NaCl, when monitored at 35 °C and pH 7. The protease activity was optimal at 2.5 M NaCl, 40°C and pH 8, with high stability at wide ranges of salinity (1-5 M NaCl), temperatures (2070 °C) and pH values (511). It was slightly improved by 5 mM CaCl2 and totally inhibited by PMSF which indicated the dominance of serine proteases. Besides, it was perfectly stable in the presence of many detergent additives and organic solvents at high concentrations. These important features make Salicola sp. strain SBJ9 protease activity a good candidate for many industrial applications such as detergency and organic synthesis.
筛选了许多新分离的嗜盐微生物用于蛋白酶生产。一种被命名为菌株SBJ9的细菌在高盐浓度下表现出重要的酶产量,然后被保留下来。16S DNA鉴定表明该菌株属于水蛭属,仅有两个参考种。在35°C和pH为7的条件下,蛋白酶产量在150 ~ 200 g/l (3.2 M) NaCl范围内较高。在2.5 M NaCl、40°C和pH 8条件下,蛋白酶活性最佳,在盐度(1-5 M NaCl)、温度(2070°C)和pH(511)范围内具有较高的稳定性。5 mM CaCl2略微改善,PMSF完全抑制,说明丝氨酸蛋白酶占优势。此外,在许多洗涤剂添加剂和高浓度有机溶剂存在下,它是完全稳定的。这些重要的特征使Salicola sp.菌株SBJ9蛋白酶活性成为许多工业应用的良好候选者,如洗涤剂和有机合成。