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http://krishi.icar.gov.in/jspui/handle/123456789/49602| Title: | Isolation, purification and characterization of a novel esterase from camel rumen metagenome |
| Other Titles: | Not Available |
| Authors: | Nilam J.Tulsani Priyaranjan Mishra Subhash J.Jakhesara Shweta Srivastava Basanti Jyotsana Nishant A.Dafalec Niteen V.Patil Hemant J.Purohit Chaitanya G.Joshia |
| ICAR Data Use Licennce: | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf |
| Author's Affiliated institute: | Department of Animal Biotechnology, College of Veterinary Science and Animal Husbandry, Anand Agricultural University, Anand, Gujarat, 388001, India Department of Animal Genetic and Breeding, College of Veterinary Science and Animal Husbandry, Anand Agricultural University, Anand, Gujarat, 388001, India Environmental Genomic Division, CSIR-National Environmental Engineering Research Institute (NEERI), Nehru Marg, Nagpur, 440020, India ICAR::National Research Centre on Camel ICAR::Central Arid Zone Research Institute Gujarat Biotechnology Research Canter, MS Building, Block B & D, 6th Floor, GH Road, Sector-11, Gandhinagar, Gujarat, 382001, India |
| Published/ Complete Date: | 2021-07-14 |
| Project Code: | Not Available |
| Keywords: | Camel rumen Metagenome Esterase Gene cloning |
| Publisher: | Elsevier |
| Citation: | Not Available |
| Series/Report no.: | Not Available; |
| Abstract/Description: | Bacterial esterases are gaining the importance in pharmaceuticals and agrochemical industries due to their excellent biocatalytic properties and a wide range of applications. In the present study, a novel gene encoding an esterase (designated as Est-CR) was identified from shotgun metagenomic sequencing data of camel rumen (Camelus dromedarius) liquor. The open reading frame consisted of 1,224bp, which showed 84.03% sequence identity to Bacteroidales bacterium, corresponding to a protein of 407 amino acids and has a catalytic domain belonging to an esterase. Est-CR belonged to family V with GLSMG domain. The purified enzyme with a molecular mass of 62.64 kDa was checked on SDS-PAGE, and its expression was confirmed by western blotting. The enzyme was active and stable over a broad range of temperature (35–65 °C), displayed the maximum activity at 50 °C and pH 7.0. Individually all metal ions inhibited the enzyme activity, while in combination, K2+, Ca2+, Mg2+ and Mn2+ metal ions enhanced the enzyme activity. The detergents strongly inhibited the activity, while EDTA (10 mM) increased the activity of the Est-CR enzyme. The enzyme showed specificity to short-chain substrates and displayed an optimum activity against butyrate ester. This novel enzyme might serve as a promising candidate to meet some harsh industrial processes enzymatic needs. |
| Description: | Not Available |
| Type(s) of content: | Research Paper |
| Sponsors: | Not Available |
| Language: | English |
| Name of Journal: | Elsevier Inc. |
| Volume No.: | 187 |
| Page Number: | 1-7 |
| Name of the Division/Regional Station: | Not Available |
| Source, DOI or any other URL: | https://doi.org/10.1016/j.pre.2021.105941 |
| URI: | http://krishi.icar.gov.in/jspui/handle/123456789/49602 |
| Appears in Collections: | NRM-CAZRI-Publication |
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