Biocatalytic Ketone Reduction - A Study on Screening and Effect of Culture Conditions on the Reduction of Selected Ketones

Kuncham, Ramprasad; Gurumurthy, K.T.; Chandan, N.; Javed, Aamir; Ashwini, L.S.; Shenoi, Rahul; Baranwal, Anup

doi:10.18052/www.scipress.com/ILNS.6.54

ILNS > Volume 6 > Biocatalytic Ketone Reduction - A Study on...

< Back to Volume

Biocatalytic Ketone Reduction - A Study on Screening and Effect of Culture Conditions on the Reduction of Selected Ketones

Full Text PDF

Abstract:

Microbial conversions are gaining importance in the synthesis of important drug metabolites and their intermediates as they are good alternative to chemical synthesis since they are enantio-selective and regio-selective and even can be carried out at ambient temperature and atmospheric pressure. Till date, biocatalytic reduction of acetophenone and its derivatives has been widely reported. In the present study, we have made an attempt to carry out the microbial bioreduction of o-hydroxyacetophenone by screening some of the selected microorganisms which were obtained from culture collection centre as well as those which are isolated in our Microbiology lab. The selected microorganisms include Aspergillus ochraceous, Aspergillus flavus, Aspergillus tubingenesis, Aspergillus niger, Rhizopus stolanifer MTCC 162, Rhizopus stolanifer MTCC 2591 and Baker’s yeast.Among the seven microorganisms screened for the bioreduction of o-hydroxyacetophenone, Baker’s yeast and Aspergillus tubingenesis showed significant bioconversion where as Aspergillus ochraceous exhibited the least bioconversion.In our earlier study it was found that Aspergillus flavus has the required bioreductase enzyme, which showed the maximum conversion of p-chloroacetophenone to p-chlorophenylethanol. Hence optimization of culture conditions to get maximum enzyme expression and hence maximum conversion was thought off. The parameters considered for the study include effect of various Carbon sources, Nitrogen source, Metal ions, incubation Temperature and media pH on enzyme expression. The optimized culture a condition at which maximum bioconversion was achieved was maltose among various carbon sources. Tryptone was found to have maximum effect among the nitrogen sources. Media pH 7.6 and incubation temperature of 35 °C was found to be favourable for maximum enzyme activity. Among various divalent metal salts, addition of magnesium sulphate to the media significantly increased the enzyme activity.

Info:

Periodical:

International Letters of Natural Sciences (Volume 6)

Pages:

54-77

DOI:

https://doi.org/10.18052/www.scipress.com/ILNS.6.54

Citation:

R. Kuncham et al., "Biocatalytic Ketone Reduction - A Study on Screening and Effect of Culture Conditions on the Reduction of Selected Ketones", International Letters of Natural Sciences, Vol. 6, pp. 54-77, 2014

Online since:

November 2013

Authors:

Ramprasad Kuncham, K.T. Gurumurthy, N. Chandan, Aamir Javed, L.S. Ashwini, Rahul Shenoi, Anup Baranwal

Keywords:

Aspergillus flavus, Aspergillus niger, Aspergillus ochraceous, Aspergillus tubingenesis, Baker’s Yeast, Rhizopus stolanifer MTCC 162, Rhizopus stolanifer MTCC 2591

Export:

RIS, BibTeX, Text

Distribution:

Open Access

This work is licensed under a
Creative Commons Attribution 4.0 International License

References:

Kaoru N., Rio Y., Tomoko M., Tadao H., Tetrahedron: Asymmetry 14 (2003) 2659-2681.

Hiltrud L., Andreas S., Biotransformations. Biotechnology, 4. http: /www. eolss. net/sample-chapters/c17/e6-58-04-06. pdf.

Elżbieta P., Dorota Ż., Department of Technology and Biotechnology of Drugs 77 (2009) 9-17.

Magdi A. M. Y, Francis F. H, Moustafa A., Mohamed S., J. Agric. & Environ. Sci. 7 (2010) 31-37.

Hanan M., Elrashied E., Trends in Applied Sciences Research 6 (2011) 121-129.

Brahmani Priyadarshini S. R, Gopal M., Sandhyavali M. S., International Journal of Pharmaceutical, Chemical and Biological Sciences 2(3) (2012) 236-241.

Aguilar-Uscanga B., Francois J. M., Letters in Applied Microbiology 37 (2003).

Xiao-Hong C., Wen-Yong L., Min-Hua Z., Thomas J. S., BMC Biotechnology 11 (2011) 110.

Chiu-yeh W., Zeng-chin L., Shiu-hsiung W., Journal of Food and Drug Analysis 16(2) (2008) 61-67.

Kyoungkeun Y., Keiko S., Naoki H., Masami T., Tsuyoshi H., Materials Transactions 5(7) (2004) 2429-34.

Neelakantam V. N., Ronan P., Applied And Environmental Microbiology 71 (2005) 2239-2243.

Sivakumar T., Sivasankara N., Shankar T., Vijayabaskar P., International Journal of Applied Biology And Pharmaceutical Technology 3 (2012) 133-143.

Sukumar M., African Journal of Environmental Science and Technology 4(7) (2010) 412-418.

Zi-Jun X., Min-Hua Z., Wen-Yong L., Bioresource Technology 100 (2009) 5560-5565.

Augusto J., Moran S., and Conceicao A., Food Technol. Biotechnol. 42 (2004) 295-303.

Hiromichi O., Toshikuni T., Takeshi S., Tetrahedron: Asymmetry 12 (2001) 2543-2555.

Adi W., Nisim H., Chrstina D., Dorith T., Yoram S., Org. Commun. 1 (2008) 9-16.

Zhong-Hua Y., Xu C., Xuan-Ke L., Guang-Hui, Wand Rong Z., Food Technol. Biotechnol. 46(3) (2008) 322-327.

S. R. Brahman, M. S. Sandhyavali, Gopal M., International journal of pharmaceutical, chemical and biological sciences 2(3) (2012) 236-241.

Yang G., Shanjing Z., and Jiangyan Xu, Journal of Molecular Catalysis B: Enzymatic 57 (2009) 83-88.

Zhang J., Gao N., J. Zhejiang Univ. Sci. B 8 (2007) 98-104.

Chanakya P., Srikanth M., Subba R. S., International Journal of Applied Biology and Pharmaceutical Technology 1 (2010) 1168-74.

Rekha K., Saran S., Jasmine I., Saxena S. K., Journal of Molecular Catalysis B: Enzymatic 40 (2006) 121-26.

Vahap Y., Aktas N., Journal of Molecular Catalysis B: Enzymatic 43 (2006) 9-14.

Vijayalakshmi and Shobha, European food research and tech. 3 (2011) 234-239. ( Received 13 November 2013; accepted 25 November 2013 ).

Show More Hide

Cited By:

This article has no citations.