<abstract xmlns="http://www.w3.org/1999/xhtml">This work reports the effects of some culture conditions on the production of glucose isomerase by Bacillus licheniformis. The bacterium was selected based on the release of 3.62 mg/mL fructose from the fermentation of glucose. Enzyme was produced using a variety of carbon substrates but the highest enzyme activity was detected in a medium containing 0.5% xylose and 1% glycerol (specific activity = 6.88 U/mg protein). Media containing only xylose or glucose gave lower enzyme productivies (specific activities= 4.60 and 2.35 U/mg protein respectively). The effects of nitrogen substrates on glucose isomerase production showed that yeast extract supported maximum enzyme activity (specific activity = 5.24 U/mg protein). Lowest enzyme activity was observed with sodium trioxonitrate (specific activity = 2.44 U/mg protein). In general, organic nitrogen substrates supported higher enzyme productivity than inorganic nitrogen substrates. Best enzyme activity was observed in the presence of Mg2+ (specific activity = 6.85 U/mg protein) while Hg2+ was inhibitory (specific activity = 1.02 U/mg protein). The optimum pH for best enzyme activity was 6.0 while optimum temperature for enzyme production was 50ºC.</abstract>

This work reports the effects of some culture conditions on the production of glucose isomerase by Bacillus licheniformis. The bacterium was selected based on the release of 3.62 mg/mL fructose from the fermentation of glucose. Enzyme was produced using a variety of carbon substrates but the highest enzyme activity was detected in a medium containing 0.5% xylose and 1% glycerol (specific activity = 6.88 U/mg protein). Media containing only xylose or glucose gave lower enzyme productivies (specific activities= 4.60 and 2.35 U/mg protein respectively). The effects of nitrogen substrates on glucose isomerase production showed that yeast extract supported maximum enzyme activity (specific activity = 5.24 U/mg protein). Lowest enzyme activity was observed with sodium trioxonitrate (specific activity = 2.44 U/mg protein). In general, organic nitrogen substrates supported higher enzyme productivity than inorganic nitrogen substrates. Best enzyme activity was observed in the presence of Mg2+ (specific activity = 6.85 U/mg protein) while Hg2+ was inhibitory (specific activity = 1.02 U/mg protein). The optimum pH for best enzyme activity was 6.0 while optimum temperature for enzyme production was 50ºC.

Studies on the production of glucose isomerase by <italic>Bacillus licheniformis</italic>

University of Nigeria, Industrial Microbiology and Biotechnology Laboratory, Department of Microbiology, Nsukka, Nigeria

Polish Journal of Chemical Technology

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Studies on the production of glucose isomerase by 

This work reports the effects of some culture conditions on the production of glucose isomerase by Bacillus licheniformis. The bacterium was selected based on...

Studies on the production of glucose isomerase by Bacillus licheniformis

Data publikacji: 19 wrz 2015

Zakres stron: 84 - 88

DOI: https://doi.org/10.1515/pjct-2015-0054

Słowa kluczowe
glucose isomerase, carbon sources, nitrogen sources, metal ions

© Ogbonnaya Nwokoro

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Studies on the production of glucose isomerase by Bacillus licheniformis

Data publikacji: 19 wrz 2015

Zakres stron: 84 - 88

DOI: https://doi.org/10.1515/pjct-2015-0054

Słowa kluczoweglucose isomerase, carbon sources, nitrogen sources, metal ions

© Ogbonnaya Nwokoro

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Słowa kluczowe
glucose isomerase, carbon sources, nitrogen sources, metal ions