| Full text | |
| Author(s): |
Maester, Thais Carvalho
[1, 2, 3]
;
Pereira, Mariana Rangel
[1, 2, 4]
;
Malaman, Aliandra M. Gibertoni
[1]
;
Borges, Janaina Pires
[5]
;
Pereira, Pamela Aparecida Maldaner
[1]
;
Lemos, Eliana G. M.
[1]
Total Authors: 6
|
| Affiliation: | [1] Sao Paulo State Univ UNESP, Dept Technol, BR-14884900 Jaboticabal, SP - Brazil
[2] Univ Sao Paulo, Inst Biomed Sci ICB 3, BR-05508900 Sao Paulo, SP - Brazil
[3] Ecobiotech Co, Supera Innovat & Technol Pk, BR-14056680 Ribeirao Preto, SP - Brazil
[4] Univ Cambridge, Dept Biochem, Cambridge CB2 1TN - England
[5] Sao Paulo State Univ UNESP, Dept Chem & Environm Sci, Inst Biosci Languages & Exact Sci, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
Total Affiliations: 5
|
| Document type: | Journal article |
| Source: | CATALYSTS; v. 10, n. 10 OCT 2020. |
| Web of Science Citations: | 0 |
| Abstract | |
Enzyme-mediated esterification reactions can be a promising alternative to produce esters of commercial interest, replacing conventional chemical processes. The aim of this work was to verify the potential of an esterase for ester synthesis. For that, recombinant lipolytic enzyme EST5 was purified and presented higher activity at pH 7.5, 45 degrees C, with a Tm of 47 degrees C. Also, the enzyme remained at least 50% active at low temperatures and exhibited broad substrate specificity toward p-nitrophenol esters with highest activity for p-nitrophenyl valerate with a K-cat/K-m of 1533 s(-1) mM(-1). This esterase exerted great properties that make it useful for industrial applications, since EST5 remained stable in the presence of up to 10% methanol and 20% dimethyl sulfoxide. Also, preliminary studies in esterification reactions for the synthesis of methyl butyrate led to a specific activity of 127.04 U center dot mg(-1). The enzyme showed higher esterification activity compared to other literature results, including commercial enzymes such as LIP4 and CL of Candida rugosa assayed with butyric acid and propanol which showed esterification activity of 86.5 and 15.83 U center dot mg(-1), respectively. In conclusion, EST5 has potential for synthesis of flavor esters, providing a concept for its application in biotechnological processes. (AU) | |
| FAPESP's process: | 11/09064-6 - Expression and structural and functional characterization of genomic sequences encoding lipolytic enzymes |
| Grantee: | Thaís Carvalho Maester Casanova |
| Support Opportunities: | Scholarships in Brazil - Doctorate |
| FAPESP's process: | 13/03568-8 - Functional and structural characterization of lipolytic enzymes identified in a metagenomic library of consortium specialized on diesel oil degradation |
| Grantee: | Eliana Gertrudes de Macedo Lemos |
| Support Opportunities: | Regular Research Grants |