Formulation of low-cost, lactose-free production medium by response surface methodology for the production of β-galactosidase using halotolerant Aspergillus tubengensis GR-1

Biocatalysis and Agricultural Biotechnology

Volumn 3, Issue 4, 2014, Pages 181-187

  Raol, Gopal G ^a   Prajapati, Vimal S ^a   Raol, B V ^b  

^a SARDAR PATEL UNIVERSITY   (India)

^b GUJARAT UNIVERSITY   (India)

Author keywords

Aspergillus tubengensis; Halotolerant; Lactose free; Response surface methodology; Solar saltern

Indexed keywords

ASPERGILLUS;

EID: 84915797199     PISSN: 18788181     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcab.2014.02.007     Document Type: Article

References (35)

1. Awan M.S., Khan S.A., Rehman Z.U., Saleem A., Rana S.M., Rajoka M.I. Influence of nitrogen sources on production of β-galactosidase by Aspergillus niger. Afr. J. Biotechnol. 2010, 9:2918-2922.
2. Cruz R., Cruz V.D., Bolete J.G., Khenafes M.O., Dorta C., Oliveira L.H.S., Ardiles E., Galli A. Production of transgalactosylated oligosaccharides (TOS) by galactosyltransferase activity from Penicillium simplicissimum. Bioresour. Technol. 1999, 70:165-171.
3. de Vries R.P., Visser J. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol. Mol. Biol. Rev. 2001, 65:497-522.
4. Fekete E., Padra J., Szentirmai A., Karaffa L. Lactose and d-galactose catabolism in the filamentous fungus Aspergillus nidulans. Acta Microbiol. Immunol. Hung. 2008, 55:119-124.
5. Felsenstein J. Confidence limits on phylogenies: an approach using the bootstrap. Evolution 1985, 39:783-791.
6. Gindy A.E., Zeinab I., Huda A. Improvement of extracellular β-galactosidase production by thermophilic fungi Chaetomium thermophile and Thermomyces lanuginosus. Aust. J. Basic Appl. Sci. 2009, 3:1925-1932.
7. Gohel V., Jiwan D., Vyas P., Chatpar H.S. Statistical optimization of chitinase production by Pantoea dispersa to enhance degradation of crustacean chitin waste. J. Microbiol. Biotechnol. 2005, 15:197-201.
8. Gupte A.M., Nair J.S. β-galactosidase production and ethanol fermentation from whey using Kluyveromyces marxianus NCIM 3551. J. Sci. Ind. Res. 2010, 69:855-859.
9. Hatzinikolaou D.G., Katsifas E., Mamma D., Karagouni A.D., Christakopoulos P., Kekos D. Modeling of the simultaneous hydrolysis-ultrafiltration of whey permeate by a thermostable ß-galactosidase from Aspergillus niger. Biochem. Eng. J. 2005, 24:161-172.
10. Isobe K., Yamashita M., Chiba S., Takahashi N., Koyama T. Characterization of new β-galactosidase from acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1. J. Biosci. Bioeng. 2013, 116:293-297.
11. Kang S.K., Cho K.K., Ahn J.K., Bok J.D., Kang S.H., Woo J.H., Lee H.G., You S.K., Choi Y.J. Three forms of thermostable lactosehydrolase from Thermus sp. IB-21: cloning, expression, and enzyme characterization. J. Biotechnol. 2005, 116:337-346.
12. Kim J.W., Rajagopal S.N. Isolation and characterization of β-galactosidase from Lactobacilus crispatus. Folia Microbiol. 2000, 45:29-34.
13. Kishore D., Kayastha A.M. A β-galactosidase from chick pea (Cicer arietinum) seeds: its purification, biochemical properties and industrial applications. Food Chem. 2012, 134:1113-1122.
14. Lu L., Xiao M., Xu X., Li Z., Li Y. A novel β-galactosidase capable of glycosyl transfer from Enterobacter agglomerans B1. Biochem. Biophys. Res. Commun. 2007, 356:78-84.
15. Mahat M.K., Illias R.M., Rahman R.A., Rashid N.A.A., Mahmood N.A.N., Hassan O. Production of cyclodextrin glucanotransferase (CGTase) from alkalophilic Bacillus sp. TSI-1: media optimization using experimental design. Enzyme Microb. Technol. 2004, 35:467-473.
16. Maksimainena M.M., Lampiob A., Mertanena M., Turunenb O., Rouvinen J. The crystal structure of acidic ß-galactosidase from Aspergillus oryzae. Int. J. Biol. Macromol. 2013, 60:109-115.
17. McKay A.M. Extracellular β-galactosidase production during growth of filamentous fungi on polygalacturonic acid. Lett. Appl. Microbiol. 1991, 12:75-77.
18. Murthy M.S.R.C., Swaminathan T., Rakshit S.K., Kosugi Y. Statistical optimization of lipase catalyzed hydrolysis of methyloleate by response surface methodology. Bioprocess Biosyst. Eng. 2000, 22:35-39.
19. Myers R.H., Montgomery D.C. Response Surface Methodology: Process and Product Optimization Using Designed Experiments 2002, 824. John Wiley and Sons, Inc., New York, NY.
20. Nagy Z., Kiss T., Szentirmai A., Biro S. Beta-galactosidase of Penicillium chrysogenum: production, purification, and characterization of the enzyme. Protein Expression Purif. 2001, 21:24-29.
21. Nair S.R., Panda T. Statistical optimization of medium components for improved synthesis of pectinase by Aspergillus niger. Bioprocess Biosyst. Eng. 1997, 16:169-173.
22. Nakayama T., Amachi T. β-galactosidase, enzymology. Encyclopedia of Bioprocess Technology-Fermentation, Biocatalysis, and Bioseparation 1999, 1291-1305. Wiley and Sons Inc., New York. M.C. Flickinger, S.W. Drew (Eds.).
23. Nizamuddin S., Sridevi A., Narasimha G. Production of β-galactosidase by Aspergillus oryzae in solid-state fermentation. Afr. J. Biotechnol. 2008, 7:1096-1100.
24. Oberoi H.S., Bansal S., Dhillon G.S. Enhanced ß-galactosidase production by supplementing whey with cauliflower waste. Int. J. Food Sci. Technol. 2008, 43:1499-1504.
25. Panesar P.S. Production of β-galactosidase from whey using Kluyveromyces marxianus. Res. J. Microbiol. 2008, 3:24-29.
26. Panesar P.S., Panesar R., Singh R.S., Kennedy J.F., Kumar H. Microbial production, immobilization and applications of β-d-galactosidase. J. Chem. Technol. Biotechnol. 2006, 81:530-543.
27. Pavani A., Gadge M.S., Prabhakar T., Rupesh P. Optimization of medium components and process parameters for the production of β-galactosidase from marine fungal isolate A. flavus. Asian J. Exp. Biol. Sci. 2011, 2:23-27.
28. Pinheiro R., Belo I., Mota M. Growth and β-galactosidase activity in cultures of Kluyveromyces marxianus under increased air pressure. Lett. Appl. Microbiol. 2003, 37:438-442.
29. Prajapati V.S., Trivedi U.B., Patel K.C. Optimization of glucoamylase production Collectotrichum sp. KCP1 using statistical methodology. Food Sci. Biotechnol. 2013, 22:31-38.
30. Raol G.G., Raol B.V., Pandya P.D. Improved production of β-Galactosidase from the mutated Aspergillus sp. on deproteinized cheese whey. Nat. Environ. Pollut. Technol. 2010, 9:699-705.
31. Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 1987, 4:406-425.
32. Sheridan P.P., Brenchley J.E. Characterization of a salt-tolerant family 42 β-galactosidase from a psychrophilic antarctic Planococcus isolate. Appl. Environ. Microbiol. 2000, 66:2438-2444.
33. Srinivas M.R.S., Nagin C., Lonsane B.K. Use of Plackett-Burman design for rapid screening of several nitrogen sources, growth/product promoters, minerals and enzyme inducers for the production of alpha-galactosidase by Aspergillus niger MRSS 234 in solid state fermentation system. Bioprocess Eng. 1994, 10:139-144.
34. Teles de Faria J., Lopes Moraes M., Del Borghi A., Converti A., Lopes Passos F.M., Minim L.A., de A.P., Vanzela F.C., Coelho Sampaio F. Use of response surface methodology to predict optimal conditions of Kluyveromyces lactis permeabilization by a physical method. Chem. Biochem. Eng. Q. 2012, 26:119-125.
35. Thigiel A.A., Deak T. Selection of strains and extraction procedures for optimum production of β-d-galactosidase from Kluyveromyces strains. Zbl. Mikrobiol. 1989, 144:465-471.