Stability and enantioselectivity of selected marine enzymes

January 29, 2021

Biocatalysis allows the synthesis of compounds in a sustainable way and can replace chemical catalysis in several processes. Biocatalysis, or catalysis mediated by enzymes, has many applications in many types of industries, such as the pharmaceutical, leather, and starch industry. The present work aimed at studying the effect of the storage temperature on the activity of the selected enzymes and understanding the factors influencing both activity and enantioselectivity of the enzymes in bioreactors with different volumes. The biocatalytic performance of two esterases from marine microorganisms origin with potential industrial application as biocatalysts, was assessed in bioreactors with 3 volumes to assess which were the most important parameters. The enantioselective resolution of the racemic substrate methyl-2-phenylpropanoate was performed with the enzyme esterase EH in an biphasic organic: aqueous system in the 3 volumes, 10, 20 and 40 mL. Variations in the mixing time and interfacial area when the reactor volume was increased, were responsible for the results of the EH enantioselectivity differences towards the substrate methyl-2-phenylpropanoate. Both activity and stability of the EH and Abo enzymes towards the substrate p-nitrophentl butyrate were assessed at different storage temperatures, -16oC and +4oC. Several experiments initially planned for this work, could not be conducted due to COVID-19

Authors in the community:

• 

  R

  Ricardo Damman Rosa Duarte Brancal

  ist190912

Supervisors of this institution:

• 

  C

  Carla da Conceição Caramujo Rocha de Carvalho

  ist30853

industrial-biotechnology - Industrial Biotechnology

eng - English

Instituto Superior Técnico