Heterologous expression of a thermophilic esterase in <Emphasis Type="Italic">Kluyveromyces</Emphasis> yeasts |
| |
Authors: | Saul Nitsche Rocha José Abrahão-Neto María Esperanza Cerdán Andreas Karoly Gombert María Isabel González-Siso |
| |
Institution: | 1.Department of Chemical Engineering,University of S?o Paulo,S?o Paulo,Brazil;2.School of Pharmaceutical Sciences,University of S?o Paulo,S?o Paulo,Brazil;3.Departamento de Bioloxía Celular e Molecular, Facultade de Ciencias,Universidade da Coru?a,Coru?a,Spain;4.Universidade Positivo,Rua Pedro Viriato Parigot de Souza,Curitiba,Brasil |
| |
Abstract: | In the present work, a thermophilic esterase from Thermus thermophilus HB27 was cloned into Kluyveromyces marxianus and into Kluyveromyces lactis using two different expression systems, yielding four recombinant strains. K. lactis showed the highest esterase expression levels (294 units per gram dry cell weight, with 65% of cell-bound enzyme) using an
episomal system with the PGK promoter and terminator from Saccharomyces cerevisiae combined with the K. lactis k1 secretion signal. K. marxianus showed higher secretion efficiency of the heterologous esterase (56.9 units per gram dry cell weight, with 34% of cell-bound
enzyme) than K. lactis. Hydrolytic activities for the heterologous esterases were maximum at pH values between 8.0 and 9.0 for both yeast species
and at temperatures of 50 °C and 45 °C for K. marxianus and K. lactis, respectively. When compared to previously published data on this same esterase produced in the original host or in S. cerevisiae, our results indicate that Kluyveromyces yeasts can be considered good hosts for the heterologous secretion of thermophilic esterases, which have a potential application
in biodiesel production or in resolving racemates. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|