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A novel thermostable lipase from Basidiomycete Bjerkandera adusta R59: characterisation and esterification studies

  • Original Paper
  • Published:
Journal of Industrial Microbiology & Biotechnology

Abstract

Microbial lipases are widely diversified in their enzymatic properties and substrate specificities, which make them very attractive for industrial application. Partially purified lipase from Bjerkandera adusta R59 was immobilized on controlled porous glass (CPG) and its properties were compared with those of the free enzyme. The free and immobilized lipases showed optimal activities at 45 and 50°C, respectively. Both enzyme forms were highly thermostable up to 60°C. The enzymes were stable at pH from 6.0 to 9.0 and their optimal pH for activity was 7.0. The free lipase was more thermostable in n-hexane than in aqueous environment. Both lipase preparations had good stabilities in non-polar solvents and were capable of hydrolysing a variety of synthetic and natural fats. Non-immobilized lipase activity was inhibited by disulphide bond reagents, serine and thiol inhibitors, while EDTA and eserine had no effect on enzyme activity. All anionic detergents tested in experiments inhibited lipase activity. The free lipase showed good stability in the presence of commercial detergents at laundry pH and temperatures. Applications of free and immobilized lipases for esterification were also presented.

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Authors and Affiliations

  1. Department of Biochemistry, Maria Curie-Sklodovska University, 20-031, Lublin, Poland

    Renata Bancerz

  2. Chair and Department of Biochemistry, Skubiszewski Medical University, 20-093, Lublin, Poland

    Grażyna Ginalska

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  1. Renata Bancerz
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  2. Grażyna Ginalska
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Correspondence to Renata Bancerz.

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Bancerz, R., Ginalska, G. A novel thermostable lipase from Basidiomycete Bjerkandera adusta R59: characterisation and esterification studies. J Ind Microbiol Biotechnol 34, 553–560 (2007). https://doi.org/10.1007/s10295-007-0232-6

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  • DOI: https://doi.org/10.1007/s10295-007-0232-6

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