Gene characterization, cloning and over-expression of two xylanases from Streptomyces padanus J103
DC Field | Value | Language |
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dc.contributor.author | 권영경 | - |
dc.contributor.author | Hettiarachchi Sachithra Amarin | - |
dc.contributor.author | 문송 | - |
dc.contributor.author | 이수진 | - |
dc.contributor.author | 강도형 | - |
dc.contributor.author | 오철홍 | - |
dc.date.accessioned | 2020-07-15T19:32:39Z | - |
dc.date.available | 2020-07-15T19:32:39Z | - |
dc.date.created | 2020-02-11 | - |
dc.date.issued | 2016-11-10 | - |
dc.identifier.uri | https://sciwatch.kiost.ac.kr/handle/2020.kiost/24343 | - |
dc.description.abstract | Xylan, a component of plant cell wall, is the most abundant non-cellulosic polysaccharide in nature. Xylanase can use to digest xylan that use for several industries such as bioethanol production, bio-bleaching of pulp, textile, production of animal feed. Streptomyces padanus strain J103 was isolated from Incheon area in Korea. Two xylanase genes (J103-x2, J103-x7) from S. padanus J103 was cloned and overexpressed in E. coli expression system. The recombinant enzymes were purified using ion-exchange chromatography with Ni+ charged column. J103-x2 and J103-x7 were 693 bp (230 aa) and 1011 bp (336 aa), separately. The J103-x2 showed the highest sequence identity of 78.4% to endo-1,4-beta-xylanase [Streptomyces sp. e14]. The J103-x7 showed the highest sequence identity of 67.1% to endo-1,4-beta-xylanase [Streptomyces sp. TN119]. Also, the molecular mass of xylanases was estimated to be 24 kDa and 35 kDa, separately. Both recombinant xylanases showed the highest activities at 60°C and pH 4.0. However their thermostability showed a significant difference. The J103-x2 was stable and retaining more than 90% of its activity after pre-incubation at 50°C for 120 min, whereas J103-x7 lost most of its activity after pre-incubation at 50°C for just 30 min.of animal feed. Streptomyces padanus strain J103 was isolated from Incheon area in Korea. Two xylanase genes (J103-x2, J103-x7) from S. padanus J103 was cloned and overexpressed in E. coli expression system. The recombinant enzymes were purified using ion-exchange chromatography with Ni+ charged column. J103-x2 and J103-x7 were 693 bp (230 aa) and 1011 bp (336 aa), separately. The J103-x2 showed the highest sequence identity of 78.4% to endo-1,4-beta-xylanase [Streptomyces sp. e14]. The J103-x7 showed the highest sequence identity of 67.1% to endo-1,4-beta-xylanase [Streptomyces sp. TN119]. Also, the molecular mass of xylanases was estimated to be 24 kDa and 35 kDa, separately. Both recombinant xylanases showed the highest activities at 60°C and pH 4.0. However their thermostability showed a significant difference. The J103-x2 was stable and retaining more than 90% of its activity after pre-incubation at 50°C for 120 min, whereas J103-x7 lost most of its activity after pre-incubation at 50°C for just 30 min. | - |
dc.description.uri | 1 | - |
dc.language | English | - |
dc.publisher | The Genetics Society of Korea | - |
dc.relation.isPartOf | International Conference of the Genetics Society of Korea 2016 | - |
dc.title | Gene characterization, cloning and over-expression of two xylanases from Streptomyces padanus J103 | - |
dc.type | Conference | - |
dc.citation.conferencePlace | KO | - |
dc.citation.endPage | 181 | - |
dc.citation.startPage | 181 | - |
dc.citation.title | International Conference of the Genetics Society of Korea 2016 | - |
dc.contributor.alternativeName | 권영경 | - |
dc.contributor.alternativeName | Amarin | - |
dc.contributor.alternativeName | 문송 | - |
dc.contributor.alternativeName | 이수진 | - |
dc.contributor.alternativeName | 강도형 | - |
dc.contributor.alternativeName | 오철홍 | - |
dc.identifier.bibliographicCitation | International Conference of the Genetics Society of Korea 2016, pp.181 | - |
dc.description.journalClass | 1 | - |