KRISHI
ICAR RESEARCH DATA REPOSITORY FOR KNOWLEDGE MANAGEMENT
(An Institutional Publication and Data Inventory Repository)
"Not Available": Please do not remove the default option "Not Available" for the fields where metadata information is not available
"1001-01-01": Date not available or not applicable for filling metadata infromation
"1001-01-01": Date not available or not applicable for filling metadata infromation
Please use this identifier to cite or link to this item:
http://krishi.icar.gov.in/jspui/handle/123456789/18481
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Hena Dhar | en_US |
dc.contributor.author | Ramesh Chand Kasana | en_US |
dc.contributor.author | Som Dutt | en_US |
dc.contributor.author | Arvind Gulati | en_US |
dc.date.accessioned | 2019-04-11T11:05:24Z | - |
dc.date.available | 2019-04-11T11:05:24Z | - |
dc.date.issued | 2015-07-30 | - |
dc.identifier.citation | 15 | en_US |
dc.identifier.issn | Not Available | - |
dc.identifier.uri | http://krishi.icar.gov.in/jspui/handle/123456789/18481 | - |
dc.description | Not Available | en_US |
dc.description.abstract | tThe endoglucanase gene designated as EG5C encoding cold active endoglucanase produced by Paenibacil-lus sp. IHB B 3084 was cloned and expressed in Escherichia coli BL21(DE3). The gene consisting of 1719 bpopen reading frame encoded a protein of 573 amino acids with a predicted molecular weight of 63.5 kDa.The presence of N-terminal catalytic domain of the glycosyl hydrolase family 5 (GH5) and C-terminalcarbohydrate binding X2 domain suggested the modular nature of the enzyme. The native signal peptideof EG5C was capable of efficiently secreting the enzyme with near equal activities in the cytoplasmic andextracellular fractions. The recombinant enzyme purified 9.46 fold to homogeneity with 22.33% yieldgave 7.758 IU/mg specific activity. The enzyme was stable over the broad pH range of 4–12 with morethan 50% residual activity. The optimal activity was at 40◦C with 70% relative activity at 5◦C. The lowtemperature activity despite the shorter linker region suggested a novel cold adaptation mechanism bythe enzyme. The enzyme displayed higher activity on carboxymethylcellulose than avicel which is usefulin maintaining the tensile strength of fiber. The efficient secretion and low temperature activity offerprospect for large-scale production and industrial application of the endoglucanase. | en_US |
dc.language.iso | English | en_US |
dc.publisher | Elsevier | en_US |
dc.relation.ispartofseries | Not Available; | - |
dc.subject | Paenibacillus sp.EndoglucanaseLow temperature active | en_US |
dc.title | Cloning and expression of low temperature active endoglucanaseEG5C from Paenibacillus sp. IHB B 3084 | en_US |
dc.type | Research Paper | en_US |
dc.publication.projectcode | Not Available | en_US |
dc.publication.journalname | International Journal of Biological Macromolecules | en_US |
dc.publication.volumeno | 81 | en_US |
dc.publication.pagenumber | 259–266 | en_US |
dc.publication.divisionUnit | Not Available | en_US |
dc.publication.sourceUrl | http://dx.doi.org/10.1016/j.ijbiomac.2015.07.060 | en_US |
dc.publication.authorAffiliation | ICAR -Central Arizd Zone Research Institute, Jodhpur | en_US |
dc.publication.authorAffiliation | CSIR-Institute of Himalayan Bioresource Technology, Palampur | en_US |
dc.ICARdataUseLicence | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf | en_US |
dc.publication.naasrating | 11.16 | en_US |
Appears in Collections: | NRM-CAZRI-Publication |
Files in This Item:
There are no files associated with this item.
Items in KRISHI are protected by copyright, with all rights reserved, unless otherwise indicated.