Please use this identifier to cite or link to this item:
https://hdl.handle.net/10321/2516
DC Field | Value | Language |
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dc.contributor.author | Khan, Faez Iqbal | en_US |
dc.contributor.author | Bisetty, Krishna | en_US |
dc.contributor.author | Singh, Suren | en_US |
dc.contributor.author | Permaul, Kugen | en_US |
dc.contributor.author | Hassan, Md. Imtaiyaz | en_US |
dc.date.accessioned | 2017-09-06T08:11:11Z | - |
dc.date.available | 2017-09-06T08:11:11Z | - |
dc.date.issued | 2015 | - |
dc.identifier.citation | Khan, F.I. et al. 2015. Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications. Extremophiles. 19: 1055–1066. | en_US |
dc.identifier.issn | 1431-0651 (print) | - |
dc.identifier.issn | 1433-4909 (online) | - |
dc.identifier.uri | http://hdl.handle.net/10321/2516 | - |
dc.description.abstract | Chitinases are ubiquitous class of extracellu-lar enzymes, which have gained attention in the past few years due to their wide biotechnological applications. The effectiveness of conventional insecticides is increasingly compromised by the occurrence of resistance; thus, chi-tinase offers a potential alternative to the use of chemical fungicides. The thermostable enzymes from thermophilic microorganisms have numerous industrial, medical, envi-ronmental and biotechnological applications due to their high stability for temperature and pH. Thermomyces lanug-inosus produced a large number of chitinases, of which chi-tinase I and II are successfully cloned and purified recently. Molecular dynamic simulations revealed that the stability of these enzymes are maintained even at higher tempera-ture. In this review article we have focused on chitinases from different sources, mainly fungal chitinase of T. lanug-inosus and its industrial application. | en_US |
dc.format.extent | 12 p | en_US |
dc.language.iso | en | en_US |
dc.publisher | Springerlink | en_US |
dc.relation.ispartof | Extremophiles (Tokyo. Internet) | en_US |
dc.subject | Chitinases | en_US |
dc.subject | TIM-barrel fold | en_US |
dc.subject | Thermomyces lanuginosus | en_US |
dc.subject | Biotechnological applications | en_US |
dc.subject | hermophilic microorganisms | en_US |
dc.subject | Thermostable enzymes | en_US |
dc.title | Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications | en_US |
dc.type | Article | en_US |
dc.publisher.uri | https://link.springer.com/content/pdf/10.1007%2Fs00792-015-0792-8.pdf | en_US |
dc.dut-rims.pubnum | DUT-005130 | en_US |
dc.description.availability | Copyright: 2015. SpringerLink. Due to copyright restrictions, only the abstract is available. For access to the full text item, please consult the publisher's website. The definitive version of the work is published in Extremophiles, Vol 19. Pp 1055-1066. https://link.springer.com/content/pdf/10.1007%2Fs00792-015-0792-8.pdf | en_US |
dc.identifier.doi | 10.1007/s00792-015-0792-8 | - |
local.sdg | SDG05 | - |
item.openairetype | Article | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
item.languageiso639-1 | en | - |
item.fulltext | No Fulltext | - |
Appears in Collections: | Research Publications (Applied Sciences) |
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