Current Science

Open Access Open Access  Restricted Access Subscription Access

Functional Characterization of Alcohol Dehydrogenase from Crabtree-Negative Yeast Komagataella (Pichia) pastoris


Affiliations
1 Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai 400 076, India
2 Department of Chemical Engineering, Indian Institute of Technology Bombay, Powai, Mumbai 400 076, India
 

Alcohol dehydrogenases (ADHs) are fermentative enzymes involved in the inter-conversion of acetaldehyde and ethanol; they are present in multiple copies in Crabtree-positive yeasts. Some have a very narrow substrate range such as acetaldehyde and ethanol, others have a broader substrate range which includes medium and long chain aldehydes and alcohols. They have also been reported in Crabtree-negative yeasts such as Kluyveromyces lactis, Scheffersomyces stipitis, Wickerhamomyces anomalus, Ogataea angusta, Komagataella (Pichia) pastoris, etc.
User
Notifications
Font Size

  • De Smidt, O., du Preez, J. C. and Albertyn, J., FEMS Yeast Res., 2008, 8, 967–978.

  • Bozzi, A., Saliola, M., Falcone, C., Bossa, F. and Martini, F., Biochim. Biophys. Acta, 1997, 1339, 133–142.

  • Passoth, V., Schafer, B., Liebel, B., Weierstall, T. and Klinner, U., Yeast, 1998, 14, 1311–1325.

  • Fredlund, E., Beerlage, C., Melin, P., Schnurer, J. and Passoth, V., Yeast, 2006, 23, 1137–1149.

  • Suwannarangsee, S. et al., Appl. Microbiol. Biotechnol., 2010, 88, 497–507.

  • Suwannarangsee, S. et al., Appl. Microbiol. Biotechnol., 2012, 96, 697–709.

  • De Schutter, K. et al., Nature Biotechnol., 2009, 27, 561–566.

  • Kurtzman, C. P., Fell, J. W. and Boekhout, T., The Yeasts, A Taxonomic Study, Elsevier, Amsterdam, 2011, 5th edn.

  • Inan, M. and Meagher, M., J. Biosci. Bioeng., 2001, 92, 337–341.

  • Agarwal, P. K., Uppada, V. and Noronha, S. B., Appl. Microbiol. Biotechnol., 2013, 97, 9439–9449.

  • Wang, Z. et al., Biotechnol. Lett., 2008, 30, 657–663.

  • Agarwal, P. K., Uppada, V., Swaminathan, A. G. and Noronha, S. B., Bioresour. Technol., 2015, 192, 90–96.

  • Inan, M., Chiruvolu, V., Eskridge, K. M., Vlasuk, G. P., Dickerson, K., Brown, S. and Meagher, M. M., Enzyme Microb. Technol., 1999, 24, 438–445.

  • Ciriacy, M., Mol. Gen. Genet., 1977, 154, 213–220.


Abstract Views: 237

PDF Views: 80




  • Functional Characterization of Alcohol Dehydrogenase from Crabtree-Negative Yeast Komagataella (Pichia) pastoris

Abstract Views: 237  |  PDF Views: 80

Authors

Vanita Uppada
Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai 400 076, India
Santosh B. Noronha
Department of Chemical Engineering, Indian Institute of Technology Bombay, Powai, Mumbai 400 076, India

Abstract


Alcohol dehydrogenases (ADHs) are fermentative enzymes involved in the inter-conversion of acetaldehyde and ethanol; they are present in multiple copies in Crabtree-positive yeasts. Some have a very narrow substrate range such as acetaldehyde and ethanol, others have a broader substrate range which includes medium and long chain aldehydes and alcohols. They have also been reported in Crabtree-negative yeasts such as Kluyveromyces lactis, Scheffersomyces stipitis, Wickerhamomyces anomalus, Ogataea angusta, Komagataella (Pichia) pastoris, etc.

References





DOI: https://doi.org/10.18520/cs%2Fv111%2Fi10%2F1596-1598