Cutinase: From molecular level to bioprocess development
β Scribed by Cristina M. L. Carvalho; Maria Raquel Aires-Barros; Joaquim M. S. Cabral
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 280 KB
- Volume
- 66
- Category
- Article
- ISSN
- 0006-3592
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β¦ Synopsis
This review analyzes the role of cutinases in nature and their potential biotechnological applications. The cloning and expression of a fungal cutinase, Fusarium solani f. pisi, in Escherichia coli and Saccharomyces cerevisiae hosts are described. The three-dimen- sional structure of this cutinase is also analyzed and its function as a lipase is discussed and compared with other lipases. The biocatalytic applications of cutinase are described taking into account the preparation of different cutinase forms and the media in which the different types of reactions have been performed, namely hydrolysis, esterification, transesterification, and resolution of racemic mixtures. The stability of cutinase preparations is discussed and, in particular, the cutinase stability in anionic reversed micelles is analyzed considering the role of hexanol as a substrate, a cosurfactant, and a stabilizer. Process development, based on the operation of cutinase reactors, is also reviewed.
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His and Lys residues contributed by the two HKD motifs.
Lipases And Phospholipases Are Key Control Elements In Mammalian Metabolism. They Share Many Common Features That Set Them Apart From Other Metabolic Enzyme Classes, Most Importantly Their Association With Biological Membranes. Their Potential As Drug Targets For The Treatment Of Metabolic Diseases
Lipases And Phospholipases Are Key Control Elements In Mammalian Metabolism. They Share Many Common Features That Set Them Apart From Other Metabolic Enzyme Classes, Most Importantly Their Association With Biological Membranes. Their Potential As Drug Targets For The Treatment Of Metabolic Diseases