I Gede Eka Perdana Putra , Maria Ulfah , Niknik Nurhayati , Is Helianti
{"title":"以玉米芯为诱导底物从转基因印尼本地卤化芽孢杆菌 CM1 共生碱性蛋白酶和木聚糖酶","authors":"I Gede Eka Perdana Putra , Maria Ulfah , Niknik Nurhayati , Is Helianti","doi":"10.1016/j.sjbs.2024.103947","DOIUrl":null,"url":null,"abstract":"<div><p>The production of corn generates a substantial amount of agro-industrial waste, with corncob accounting for a significant portion of this waste. In this study, we focused on utilizing corncob as a carbon source and inducer to simultaneously produce two valuable industrial enzymes, protease, and xylanase, using a recombinant strain of <em>B. halodurans</em> CM1. Interestingly, xylan-rich corncob not only enhanced the xylanase activity but also induced protease activity of the modified <em>B. halodurans</em> CM1 strain. The effect of corncob concentration on the coproduction of protease and xylanase was investigated. Corncob with 6 % concentration induced protease activity of 1020.7 U/mL and xylanase activity of 502.8 U/mL in a 7 L bioreactor under the condition of 1 vvm aeration, 250 rpm agitation, 37 °C temperature, initial pH 9.0, and 40 h incubation period. The protease produced was an alkalothermophilic enzyme whose highest activity was at pH 12 and 50 °C, and it belonged to a serine protease family. This alkalothermophilic protease’s activity to some degree was reduced by Co<sup>2+</sup>, Mg<sup>2+</sup>, Fe<sup>2+</sup>, Zn<sup>2+</sup>, and K<sup>+</sup>, but enhanced by Ca<sup>2+</sup> and Ni<sup>2+</sup> (at 5 mM). The protease was stable even under the presence of a 15 % concentration of acetone, DMSO, ethanol, and isopropyl alcohol. The protease activity at 30 °C was not considerably changed by the presence of detergent, indicating excellent potential as a washing detergent additive. According to these findings, corncob has the potential to be a substrate for the coproduction of protease and xylanase, which have a wide range of industrial uses.</p></div>","PeriodicalId":21540,"journal":{"name":"Saudi Journal of Biological Sciences","volume":"31 4","pages":"Article 103947"},"PeriodicalIF":4.4000,"publicationDate":"2024-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1319562X24000251/pdfft?md5=30d60f0d31ba2a8c12688e5da7c10d31&pid=1-s2.0-S1319562X24000251-main.pdf","citationCount":"0","resultStr":"{\"title\":\"Coproduction of alkaline protease and xylanase from genetically modified Indonesian local Bacillus halodurans CM1 using corncob as an inducing substrate\",\"authors\":\"I Gede Eka Perdana Putra , Maria Ulfah , Niknik Nurhayati , Is Helianti\",\"doi\":\"10.1016/j.sjbs.2024.103947\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The production of corn generates a substantial amount of agro-industrial waste, with corncob accounting for a significant portion of this waste. In this study, we focused on utilizing corncob as a carbon source and inducer to simultaneously produce two valuable industrial enzymes, protease, and xylanase, using a recombinant strain of <em>B. halodurans</em> CM1. Interestingly, xylan-rich corncob not only enhanced the xylanase activity but also induced protease activity of the modified <em>B. halodurans</em> CM1 strain. The effect of corncob concentration on the coproduction of protease and xylanase was investigated. Corncob with 6 % concentration induced protease activity of 1020.7 U/mL and xylanase activity of 502.8 U/mL in a 7 L bioreactor under the condition of 1 vvm aeration, 250 rpm agitation, 37 °C temperature, initial pH 9.0, and 40 h incubation period. The protease produced was an alkalothermophilic enzyme whose highest activity was at pH 12 and 50 °C, and it belonged to a serine protease family. This alkalothermophilic protease’s activity to some degree was reduced by Co<sup>2+</sup>, Mg<sup>2+</sup>, Fe<sup>2+</sup>, Zn<sup>2+</sup>, and K<sup>+</sup>, but enhanced by Ca<sup>2+</sup> and Ni<sup>2+</sup> (at 5 mM). The protease was stable even under the presence of a 15 % concentration of acetone, DMSO, ethanol, and isopropyl alcohol. The protease activity at 30 °C was not considerably changed by the presence of detergent, indicating excellent potential as a washing detergent additive. According to these findings, corncob has the potential to be a substrate for the coproduction of protease and xylanase, which have a wide range of industrial uses.</p></div>\",\"PeriodicalId\":21540,\"journal\":{\"name\":\"Saudi Journal of Biological Sciences\",\"volume\":\"31 4\",\"pages\":\"Article 103947\"},\"PeriodicalIF\":4.4000,\"publicationDate\":\"2024-02-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.sciencedirect.com/science/article/pii/S1319562X24000251/pdfft?md5=30d60f0d31ba2a8c12688e5da7c10d31&pid=1-s2.0-S1319562X24000251-main.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Saudi Journal of Biological Sciences\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1319562X24000251\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"Agricultural and Biological Sciences\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Saudi Journal of Biological Sciences","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1319562X24000251","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"Agricultural and Biological Sciences","Score":null,"Total":0}
Coproduction of alkaline protease and xylanase from genetically modified Indonesian local Bacillus halodurans CM1 using corncob as an inducing substrate
The production of corn generates a substantial amount of agro-industrial waste, with corncob accounting for a significant portion of this waste. In this study, we focused on utilizing corncob as a carbon source and inducer to simultaneously produce two valuable industrial enzymes, protease, and xylanase, using a recombinant strain of B. halodurans CM1. Interestingly, xylan-rich corncob not only enhanced the xylanase activity but also induced protease activity of the modified B. halodurans CM1 strain. The effect of corncob concentration on the coproduction of protease and xylanase was investigated. Corncob with 6 % concentration induced protease activity of 1020.7 U/mL and xylanase activity of 502.8 U/mL in a 7 L bioreactor under the condition of 1 vvm aeration, 250 rpm agitation, 37 °C temperature, initial pH 9.0, and 40 h incubation period. The protease produced was an alkalothermophilic enzyme whose highest activity was at pH 12 and 50 °C, and it belonged to a serine protease family. This alkalothermophilic protease’s activity to some degree was reduced by Co2+, Mg2+, Fe2+, Zn2+, and K+, but enhanced by Ca2+ and Ni2+ (at 5 mM). The protease was stable even under the presence of a 15 % concentration of acetone, DMSO, ethanol, and isopropyl alcohol. The protease activity at 30 °C was not considerably changed by the presence of detergent, indicating excellent potential as a washing detergent additive. According to these findings, corncob has the potential to be a substrate for the coproduction of protease and xylanase, which have a wide range of industrial uses.
期刊介绍:
Saudi Journal of Biological Sciences is an English language, peer-reviewed scholarly publication in the area of biological sciences. Saudi Journal of Biological Sciences publishes original papers, reviews and short communications on, but not limited to:
• Biology, Ecology and Ecosystems, Environmental and Biodiversity
• Conservation
• Microbiology
• Physiology
• Genetics and Epidemiology
Saudi Journal of Biological Sciences is the official publication of the Saudi Society for Biological Sciences and is published by King Saud University in collaboration with Elsevier and is edited by an international group of eminent researchers.