An alkaline and surfactant-tolerant lipase from Trichoderma lentiforme ACCC30425 with high application potential in the detergent industry
| Autor: | Ma Rui, Gu Jingang, Li Shigui, Bin Yao, Gong Mingbo, Yingguo Bai, Wang Yuzhou |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0106 biological sciences
0301 basic medicine Detergent Triton x100 lcsh:Biotechnology Biophysics lcsh:QR1-502 01 natural sciences Applied Microbiology and Biotechnology Trichoderma lentiforme lcsh:Microbiology law.invention Pichia pastoris 03 medical and health sciences Pulmonary surfactant law 010608 biotechnology lcsh:TP248.13-248.65 Lipase Incubation Chromatography biology Chemistry biology.organism_classification Alkaline lipase 030104 developmental biology Recombinant DNA biology.protein Heterologous expression |
| Zdroj: | AMB Express, Vol 8, Iss 1, Pp 1-11 (2018) |
| ISSN: | 2191-0855 |
| DOI: | 10.1186/s13568-018-0618-z |
| Popis: | Alkaline lipases with adaptability to low temperatures and strong surfactant tolerance are favorable for application in the detergent industry. In the present study, a lipase-encoding gene, TllipA, was cloned from Trichoderma lentiforme ACCC30425 and expressed in Pichia pastoris GS115. The purified recombinant TlLipA was found to have optimal activities at 50 °C and pH 9.5 and retain stable over the pH range of 6.0–10.0 and 40 °C and below. When using esters of different lengths as substrates, TlLipA showed preference for the medium length p-nitrophenyl octanoate. In comparison to commercial lipases, TlLipA demonstrated higher tolerance to various surfactants (SDS, Tween 20, and Triton X100) and retained more activities after incubation with Triton X100 for up to 24 h. These favorable characteristics make TlLipA prospective as an additive in the detergent industry. |
| Databáze: | OpenAIRE |
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