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Investigation on Extracellular Lipase Production by Aspergillus japonicus Isolated from the Paper Nest of Ropalidia marginata


Affiliations
1 Centre for Advanced Studies in Botany, University of Madras, Guindy Campus, Chennai 600 025, Tamil Nadu, India
 

Aspergillus japonicus isolated from the paper nest of Ropalidia marginata was screened for its extracellular lipase production. Maximum lipase activity (120 U/ml) was achieved by manipulating the culture environment. The optimum pH was 7.5 and the temperature was 40°C. Sucrose served as the best carbon source whereas peptone was the best nitrogen source for lipase production. An animal fat, pig fat in the culture medium enhanced lipase production. These investigations will be helpful in further scaling-up processes of this industrial enzyme. Owing to many applications in high-value syntheses and as bulk enzymes, lipases have high impact on bioprocessing.

Keywords

Aspergillus japonicus, Paper Nest, Pig Fat, Ropalidia marginata, Lipase, Tween-20
User

  • Agres (1994) Statistical software version 3.01. Pascal International solutions, USA.

  • Choo DW, kurihara T, Suzuki T, Soda K and Esaki NA (1998) Cold adapted lipase of an Alaskan psychrotroph, Pseudomonas sp., Strain B 11-1: Gene cloning and enzyme purification and characterization. Appl. Environ. Microbiol. 64, 486-491.

  • Elibol M and Ozer D (2001) Influence of oxygen transfer on lipase production by Rhizopus arrhizus. Proc. Biochem. 36, 325-329.

  • Ferreira-Costa MA and Peralta RM (1999) Production of lipase by soil fungi and partial characterization lipase from a selected strain (Penicillium wortmanii). J. Basic. Microbiol. 39, 11-15.

  • Fu X, Zhu X, Gao K and Duan J (1995) Oil and fat hydrolysis with lipase from Aspergillus sp. J. American Oil Chem. Soc. 72, 527–531.

  • George E, Tamerler C, Martinez A, Martinez MJ and Keshavarz T (1999) Influence of growth composition on the lipolytic enzyme activity of Ophiostoma piliferm. J. Chem. Technol. Biotech. 74, 137-140.

  • Gitlesen T, Bauer M and Adlercreutz P (1997) Adsorption of Lipase on polypropylene powder. Biochem. Biophys. Acta. 1345, 188-196.

  • Gombert AK, Pintoal-Castilho LR and Freirc DMG (1999) Lipase by Penicillium restrictum in solid state fermentation using Babassu oil cake as substrate. Proc. Biochem. 35, 85-90.

  • Gulati R, Jasmine ISAR, Vineet K, Parsad A, Parmar V and Saxena K (2005) Production of a novel alkaline lipase by Fusarium globulosum using Neem oil, and its applications. Pure Appl. Chem. 77, 251-262.

  • Hoshino T, Mizutani A, Shimizu S, Hidaka H and Yamane T (1991) Calcium ion regulates the release of lipase of Fusarium oxysporum. J. Biochem. 110, 457-461.

  • Jaeger KE and Reetz MT (1998) Microbial lipases form versatile tools for biotechnology. Trend Biotechnol. 16, 396- 403.

  • Jonsson U and Snygg BG (1974) Lipase production and activity as a function of incubation time, pH and temperature of four lipolytic microorganisms. J. Appl. Bacteriol. 37(4), 571–581.

  • Lockington R, Rodbourn L, Barnett S, Carter C and Kelly J (2002) Regulation by carbon and nitrogen sources of a family of cellulases in Aspergillus nidulans. Fungi Genetics Biol. 37, 190-196.

  • Maia MMD, Heasley A, CamargodeMorais MM, Melo EH, Morais MA, Jr. Ledingham WM and Lima FJL (2001) Effect of culture conditions on lipase production by Fusarium solani in batch fermentation. Biores. Technol. 76, 23–27.

  • Mateos DJC, Rodrguez JA, Roussos S, Cordova J, Abousalham A, Carriere F and Baratti J (2006) Lipase from the thermotolerant fungus Rhizopus homothallicus is more thermostable when produced using solid state fermentation than liquid fermentation procedures. Enz. Microbial. Technol. 39, 1042-1050.

  • Muralidhar RV, Marchant R and Nigam P (2001) Lipases in racemic resolutions. J. Chem. Technol. Biotechnol. 76, 3-8.

  • Prescott LM, Harley JP and Klein DA (1993) Microbiology, Second edn. Wm. C. Brown Publishers, p. 912.

  • Roberts RG, Morrison WH and Robertson JA (1987) Extracellular lipase production by fungi from sunflower seed. Mycologia. 79, 265-273.

  • Snellman EA and Colwell RR (2004) Acinetobacter lipase: molecular biology, biochemical properties and biotechnological potential. J. Industrial Microbiol. Biotechnol. 31, 391-400.

  • Valeria MG, Lima-Nadia K, Maria-Inez M, Sarquis-David A, Mitchell-Luiz P and Ramos–Jose D (2003) Production of Lipase by Penicillium aurantiogriseum. Food Technol. Biotechnol. 41, 105–110.

  • Winkler VK and Stuckmann M (1979) Glycogen, hyaluronate and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. J. Bacteriol. 138, 663-670.

  • Yadav RP, Saxena RK, Gupta R and Davidson WS (1998) Lipase production by Aspergillus and Penicillium spp. Folia Microbiol. 43(4), 373-378.


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  • Investigation on Extracellular Lipase Production by Aspergillus japonicus Isolated from the Paper Nest of Ropalidia marginata

Abstract Views: 591  |  PDF Views: 174

Authors

A. Jayaprakash
Centre for Advanced Studies in Botany, University of Madras, Guindy Campus, Chennai 600 025, Tamil Nadu, India
P. Ebenezer
Centre for Advanced Studies in Botany, University of Madras, Guindy Campus, Chennai 600 025, Tamil Nadu, India

Abstract


Aspergillus japonicus isolated from the paper nest of Ropalidia marginata was screened for its extracellular lipase production. Maximum lipase activity (120 U/ml) was achieved by manipulating the culture environment. The optimum pH was 7.5 and the temperature was 40°C. Sucrose served as the best carbon source whereas peptone was the best nitrogen source for lipase production. An animal fat, pig fat in the culture medium enhanced lipase production. These investigations will be helpful in further scaling-up processes of this industrial enzyme. Owing to many applications in high-value syntheses and as bulk enzymes, lipases have high impact on bioprocessing.

Keywords


Aspergillus japonicus, Paper Nest, Pig Fat, Ropalidia marginata, Lipase, Tween-20

References





DOI: https://doi.org/10.17485/ijst%2F2010%2Fv3i2%2F29660