Zohra Yasmine Zater , Mohamed Merzoug , Mustafa Ozkan Baltaci , Svetoslav Dimitrov Todorov , Ahmet Adiguzel , Salima Roudj
{"title":"新型酪蛋白溶解蛋白酶单一突变对戊糖乳杆菌生长性能的影响","authors":"Zohra Yasmine Zater , Mohamed Merzoug , Mustafa Ozkan Baltaci , Svetoslav Dimitrov Todorov , Ahmet Adiguzel , Salima Roudj","doi":"10.1016/j.procbio.2024.06.025","DOIUrl":null,"url":null,"abstract":"<div><p>The caseinolytic protease (ClpP)-producing strain CHFM, isolated from Algerian goat milk, was identified as <em>Lactiplantibacillus pentosus</em> through 16 S rRNA sequence analysis. The optimal conditions for ClpP expression by <em>Lpb. pentosus</em> CHFM were determined in a modified MRS medium, where peptone was replaced with casein. The most favourable conditions were a pH of 8.0, a temperature between 25°C and 55°C, and an incubation period of 48 h. PCR screening and subsequent cloning and sequencing of the ClpP-encoding gene from the <em>Lpb. pentosus</em> CHFM genome revealed two conservative substitutions: threonine to serine at position 161, and aspartic acid to glutamic acid at position 182. Bioinformatic analysis indicated an instability index value of 40.51 for ClpP CHFM, suggesting stability, with an alpha-helix being the predominant secondary structure element, followed by a random coil. The aliphatic index was 97.60, indicating thermal stability. The GRAVY index was −0.23, suggesting enhanced interaction with water. The molecular weight was found to be 25.5 kDa with an isoelectric point (pI) of 4.78. The structural and docking analysis demonstrated that ClpP CHFM possesses the ability to hydrolyze αS1-casein.</p></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":null,"pages":null},"PeriodicalIF":3.7000,"publicationDate":"2024-06-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Impact of a novel caseinolytic protease single mutation on Lactiplantibacillus pentosus growth performance\",\"authors\":\"Zohra Yasmine Zater , Mohamed Merzoug , Mustafa Ozkan Baltaci , Svetoslav Dimitrov Todorov , Ahmet Adiguzel , Salima Roudj\",\"doi\":\"10.1016/j.procbio.2024.06.025\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The caseinolytic protease (ClpP)-producing strain CHFM, isolated from Algerian goat milk, was identified as <em>Lactiplantibacillus pentosus</em> through 16 S rRNA sequence analysis. The optimal conditions for ClpP expression by <em>Lpb. pentosus</em> CHFM were determined in a modified MRS medium, where peptone was replaced with casein. The most favourable conditions were a pH of 8.0, a temperature between 25°C and 55°C, and an incubation period of 48 h. PCR screening and subsequent cloning and sequencing of the ClpP-encoding gene from the <em>Lpb. pentosus</em> CHFM genome revealed two conservative substitutions: threonine to serine at position 161, and aspartic acid to glutamic acid at position 182. Bioinformatic analysis indicated an instability index value of 40.51 for ClpP CHFM, suggesting stability, with an alpha-helix being the predominant secondary structure element, followed by a random coil. The aliphatic index was 97.60, indicating thermal stability. The GRAVY index was −0.23, suggesting enhanced interaction with water. The molecular weight was found to be 25.5 kDa with an isoelectric point (pI) of 4.78. The structural and docking analysis demonstrated that ClpP CHFM possesses the ability to hydrolyze αS1-casein.</p></div>\",\"PeriodicalId\":20811,\"journal\":{\"name\":\"Process Biochemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":3.7000,\"publicationDate\":\"2024-06-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Process Biochemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1359511324002125\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Process Biochemistry","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1359511324002125","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Impact of a novel caseinolytic protease single mutation on Lactiplantibacillus pentosus growth performance
The caseinolytic protease (ClpP)-producing strain CHFM, isolated from Algerian goat milk, was identified as Lactiplantibacillus pentosus through 16 S rRNA sequence analysis. The optimal conditions for ClpP expression by Lpb. pentosus CHFM were determined in a modified MRS medium, where peptone was replaced with casein. The most favourable conditions were a pH of 8.0, a temperature between 25°C and 55°C, and an incubation period of 48 h. PCR screening and subsequent cloning and sequencing of the ClpP-encoding gene from the Lpb. pentosus CHFM genome revealed two conservative substitutions: threonine to serine at position 161, and aspartic acid to glutamic acid at position 182. Bioinformatic analysis indicated an instability index value of 40.51 for ClpP CHFM, suggesting stability, with an alpha-helix being the predominant secondary structure element, followed by a random coil. The aliphatic index was 97.60, indicating thermal stability. The GRAVY index was −0.23, suggesting enhanced interaction with water. The molecular weight was found to be 25.5 kDa with an isoelectric point (pI) of 4.78. The structural and docking analysis demonstrated that ClpP CHFM possesses the ability to hydrolyze αS1-casein.
期刊介绍:
Process Biochemistry is an application-orientated research journal devoted to reporting advances with originality and novelty, in the science and technology of the processes involving bioactive molecules and living organisms. These processes concern the production of useful metabolites or materials, or the removal of toxic compounds using tools and methods of current biology and engineering. Its main areas of interest include novel bioprocesses and enabling technologies (such as nanobiotechnology, tissue engineering, directed evolution, metabolic engineering, systems biology, and synthetic biology) applicable in food (nutraceutical), healthcare (medical, pharmaceutical, cosmetic), energy (biofuels), environmental, and biorefinery industries and their underlying biological and engineering principles.