Isolation, purification and characterization of a novel esterase from camel rumen metagenome
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Title |
Isolation, purification and characterization of a novel esterase from camel rumen metagenome
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Creator |
N.V.Patil
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Subject |
Camel rumen,Metagenome,Esterase,Gene cloning
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Description |
Not Available
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 mo-lecular 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. |
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Date |
2021-10-28T10:32:51Z
2021-10-28T10:32:51Z 2021-7-14 |
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Type |
Research Paper
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Identifier |
Not Available
1046-5928 http://krishi.icar.gov.in/jspui/handle/123456789/66462 |
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Language |
English
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Publisher |
Not Available
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