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A Novel Low-Temperature Alkaline Lipase from Acinetobacter johnsonii LP28 Suitable for Detergent Formulation

Hai Kuan Wang ; Key Laboratory of Industrial Microbiology, Ministry of Education, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, PR China
Jing Shao ; Key Laboratory of Industrial Microbiology, Ministry of Education, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, PR China
Yu Jie Wei ; Key Laboratory of Industrial Microbiology, Ministry of Education, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, PR China
Jie Zhang ; Key Laboratory of Industrial Microbiology, Ministry of Education, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, PR China
Wei Qi ; Key Laboratory of Industrial Microbiology, Ministry of Education, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, PR China

Puni tekst: engleski, pdf (346 KB) str. 96-102 preuzimanja: 1.348* citiraj
APA 6th Edition
Wang, H.K., Shao, J., Wei, Y.J., Zhang, J. i Qi, W. (2011). A Novel Low-Temperature Alkaline Lipase from Acinetobacter johnsonii LP28 Suitable for Detergent Formulation. Food Technology and Biotechnology, 49 (1), 96-102. Preuzeto s https://hrcak.srce.hr/65626
MLA 8th Edition
Wang, Hai Kuan, et al. "A Novel Low-Temperature Alkaline Lipase from Acinetobacter johnsonii LP28 Suitable for Detergent Formulation." Food Technology and Biotechnology, vol. 49, br. 1, 2011, str. 96-102. https://hrcak.srce.hr/65626. Citirano 21.10.2021.
Chicago 17th Edition
Wang, Hai Kuan, Jing Shao, Yu Jie Wei, Jie Zhang i Wei Qi. "A Novel Low-Temperature Alkaline Lipase from Acinetobacter johnsonii LP28 Suitable for Detergent Formulation." Food Technology and Biotechnology 49, br. 1 (2011): 96-102. https://hrcak.srce.hr/65626
Harvard
Wang, H.K., et al. (2011). 'A Novel Low-Temperature Alkaline Lipase from Acinetobacter johnsonii LP28 Suitable for Detergent Formulation', Food Technology and Biotechnology, 49(1), str. 96-102. Preuzeto s: https://hrcak.srce.hr/65626 (Datum pristupa: 21.10.2021.)
Vancouver
Wang HK, Shao J, Wei YJ, Zhang J, Qi W. A Novel Low-Temperature Alkaline Lipase from Acinetobacter johnsonii LP28 Suitable for Detergent Formulation. Food Technology and Biotechnology [Internet]. 2011 [pristupljeno 21.10.2021.];49(1):96-102. Dostupno na: https://hrcak.srce.hr/65626
IEEE
H.K. Wang, J. Shao, Y.J. Wei, J. Zhang i W. Qi, "A Novel Low-Temperature Alkaline Lipase from Acinetobacter johnsonii LP28 Suitable for Detergent Formulation", Food Technology and Biotechnology, vol.49, br. 1, str. 96-102, 2011. [Online]. Dostupno na: https://hrcak.srce.hr/65626. [Citirano: 21.10.2021.]

Sažetak
A strain LP28 that produces alkaline and low-temperature lipase was isolated from the soil collected from the Bay of Bohai, PR China and identified as Acinetobacter johnsonii using 16S rDNA sequencing. The lipase was purified to homogeneity by centrifugation, followed by ammonium sulphate precipitation, dialysis, ion exchange chromatography on cellulose DE-52 and gel filtration chromatography on Sephadex G-75. The enzyme was purified about 34-fold with a final yield of 13 % and the relative molecular mass of the enzyme was determined to be 53 kDa by SDS-PAGE. The purified enzyme exhibited maximum activity at 30 °C and pH=9.0, and retained 94.53 % of its maximum activity at 20 °C. The enzyme was stable at 50 °C and retained 80.9 % of its original activity for 30 min. It was also highly stable in a pH range of 8.0–11.0. The enzyme hydrolyzed a wide range of oils and showed a high level of lipase activity in hydrolyzing tributyrin. The enzyme activity was promoted in the presence of Na+, Ca2+, K+, Mg2+ and sodium citrate. Ba2+, Mn2+, Cr3+ and Co2+ did not affect the enzyme activity, whereas the presence of Al3+, Cu2+, Fe2+, Fe3+, Zn2+ and EDTA reduced the enzyme activity. Regarding the stability of detergent process, the enzyme was highly stable in the presence of various oxidizing agents, some commercial detergents and alkaline protease, and its activity was also promoted by most of the surfactants, viz. Tween 20, Tween 80, sodium cholate, sodium taurocholate and saponin. For these characteristics, the lipase from Acinetobacter johnsonii LP28 showed good potential as an additive in laundry detergent formulation.

Ključne riječi
Acinetobacter johnsonii; alkaline lipase; low-temperature lipase; detergent formulation

Hrčak ID: 65626

URI
https://hrcak.srce.hr/65626

[hrvatski]

Posjeta: 1.803 *