Volume 12, Issue 2 (2022)                   JMBS 2022, 12(2): 51-66 | Back to browse issues page

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Ariaeenejad S, Maleki M, Nooshi Nedamani S, Kavousi K, Hosseini salekdeh G. Identification, cloning, and expression of the novel recombinant xylanase with stable structure from the sheep rumen microbiota. JMBS 2022; 12 (2) :51-66
URL: http://biot.modares.ac.ir/article-22-42005-en.html
1- Department of Systems and Synthetic Biology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREEO), Karaj, Iran. , shariaee@gmail.com
2- Department of Systems and Synthetic Biology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREEO), Karaj, Iran.
3- Laboratory of Complex Biological Systems and Bioinformatics (CBB), Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran, Department of Systems and Synthetic Biology, Agricultural Biotechnology Research Institute of Iran (ABRII), Karaj, Iran.
Abstract:   (1802 Views)
Enzymes play an essential role in catalyzing the reactions for multiple industrial applications. One of these critical industries with a worldwide application is paper and pulp, which is cost-effective in increasing attention. Xylanases are potential enzymes that proved their abilities in a broad range of applications, specifically in the paper and pulp industry as a biobleaching agent and dye removal biocatalyst. In these decades, the production of novel enzymes from natural sources is conceivable, especially with applying the culture-independent method of metagenome. This practical approach provides the opportunity to identify the novel enzymes from uncultivable microbial diversities. Concerning the importance of the thermostable enzymes for industrial applications and their better action in harsh conditions, this study aimed to identify novel thermostable xylanase from metagenomic data of sheep rumen by applying the in-silico screening. The thermostable xylanase was extracted from the ruminal DNA and after cloning and expression named PersiXyn5. The enzymeschr('39') kinetic parameters, including Km, Vmax, and its specific activity, were examined. The enzyme was optimally active at 80  and pH 8 and could retain 58% of its maximum activity after 2h of incubation at 90 . The thermostable, alkali PersiXyn5 was an efficient enzyme in the paper industry and poultry feed and fuel applications.
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Article Type: Original Research | Subject: Microbial biotechnology
Received: 2020/04/11 | Accepted: 2021/01/11 | Published: 2022/01/30

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