Microbial Biotechnology

Process Biotechnology

Electronic Journal of Biotechnology ISSN: 0717-3458 Vol. 12 No. 4, Issue of October 15, 2009
© 2009 by Pontificia Universidad Católica de Valparaíso -- Chile Received May 25, 2008 / Accepted September 6, 2009
DOI: 10.2225/vol12-issue4-fulltext-8

Culture conditions for the production of α-galactosidase by Aspergillus parasiticus MTCC-2796: a novel source 

Kumar Shivam
Department of Biotechnology
D.D.U. Gorakhpur University
Gorakhpur, India

Chandra Prakash Mani Tripathi
Department of Zoology
D.D.U. Gorakhpur University
Gorakhpur, India

Sarad Kumar Mishra*
Department of Biotechnology
D.D.U. Gorakhpur University
Gorakhpur 273009, India
E-mail: saradmishra5@rediffmail.com

*Corresponding author

Financial support: Deen Dayal Upadhyay Gorakhpur University, Gorakhpur, India.

Keywords: Aspergillus parasiticus, α-galactosidase, culture condition, submerged fermentation.


MTCC: microbial type culture collection
oNPG: o-nitrophenyl-α-D-galactopyranoside
SmF: submerged fermentation

Abstract   Full Text

Aspergillus parasiticus microbial type culture collection (MTCC)-2796, a new source of α-galactosidase is an efficient producer of enzyme in basic medium under submerged fermentation conditions. Maximum α-galactosidase production (156.25 Uml-1) was obtained when the basic medium is supplemented with galactose (0.5% w/v) and raffinose (0.5% w/v) as carbon source and yeast extract as nitrogen source. Enzyme production was also enhanced considerably in the presence of wheat bran (1.0% w/v). Enzyme secretion was strongly inhibited by the presence of Hg2+, Cu2+, and Co2+ in the medium and to some extent by Zn2+ and Ni2+, while marginal increase in the enzyme production was observed when Mg2+ and Mn2+ were added in the medium. Among amino acids checked (aparagine, cysteine, glutamine, leucine and proline), glutamine (1 mM) was found to be an enhancer for the enzyme production. The temperature and pH range for the production of enzyme were 25ºC to 35ºC and 6.5 to 7.5, respectively with maximum activity (50 Uml-1) at 30ºC and pH 6.5 under static fermentation condition.

Supported by UNESCO / MIRCEN network