Cutinase structure, function and biocatalytic applications

Abstract

This review analyses the role of cutinases in nature and their potential biotechnological applications. The cloning and expression of a fungal cutinase from Fusarium solani f. pisi, in Escherichia coli and Saccharomyces cerevisiae hosts are described. The three dimensional structure of this cutinase is also analysed and its function as a lipase 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 where the different types of enzymatic reactions have been performed, namely hydrolysis, esterification, transesterification and resolution of racemic mixtures. The stability of cutinase preparations is discussed, particularly in anionic reversed micelles considering the role of hexanol as substrate, co-surfactant and stabilizer. Process development based on the operation of cutinase reactors is also reviewed.Cutinases are hydrolytic enzymes that degrade cutin, the cuticular polymer of higher plants, which is a polyester composed of hydroxy and epoxy fatty acids (Purdy and Kolattukudy, 1975). The fatty acids of cutin are usually n-C 16 and n-C 18 and contain one to three hydroxyl groups. Ester bonds predominate in the cutins, although peroxide bridges and ether linkages have also been presented.Cutin plays a key role in protection against the entry of pathogens into plants, and its enzymatic degradation has proved to be one of the first steps in the infection process.

NovelCoprinopsis cinereaPolyesterase That Hydrolyzes Cutin and Suberin

“…It can be deduced from the determined size that the introns of the CcCUT1 gene model seem to be correctly spliced in T. reesei. The determined CcCUT1 masses are close to those of most fungal cutinases, 22 to 25 kDa (5,25). However, some cutinases are larger, such as B. cinereus cutinase, with a molecular mass of 40.8 kDa (18).…”

“…The active sites of all biochemically well-characterized cutinases are composed of serine, aspartate, and histidine residues, which form a catalytic triad similar in arrangement to those of serine proteinases and several lipases (5). A short consensus sequence around the active serine residue of cutinases is Gly-Tyr-Ser-Gln-Gly (5).…”

Purification and Characterization of Mycobacterial Phospholipase A: an Activity Associated with Mycobacterial Cutinase

“…Phospholipase activity has not been previously associated with cutinases. Cutinase research primarily focuses on phytopathogenic fungi, on the use of cutinase in laundry agents to remove plant stains, and on the use of cutinase to degrade biodegradable plastics (4,5,10). Fusarium solani cutinase is perhaps the most well studied cutinase (14).…”

Cutinases fúngicas: propriedades e aplicações industriais

“…Tratamentos empregando agentes alcalinos fortes melhoram a hidrofilicidade e reatividade química de tais fibras, mas tais processos são de difícil controle, freqüentemente resultando em graus variáveis de perda de resistência do tecido. 8,49,50 Além disso, a grande quantidade de hidróxido de sódio e as altas temperaturas necessárias tornam o processo pouco atraente do ponto de vista ambiental. A modificação das propriedades das fibras em busca de menor hidrofobicidade deve limitar-se à superfície, sem alterar as propriedades do interior.…”