caa a22 4500 605500681 CHVBK 20210128100557.0 cr unu---uuuuu 210128e20150601xx s 000 0 eng 10.1007/s00253-015-6596-z doi (NATIONALLICENCE)springer-10.1007/s00253-015-6596-z Nyyssölä Antti VTT Technical Research Centre of Finland Ltd., Industrial Biotechnology, P.O. Box 1000, 02044, Espoo, Finland aut Which properties of cutinases are important for applications? [Elektronische Daten] [Antti Nyyssölä] Cutinases (EC 3.1.1.74) are extracellular enzymes that belong to α/β hydrolases. They are serine esterases with the classical Ser-His-Asp triad similar to several lipases and serine proteases. In nature, cutinases catalyse the hydrolysis of the polyesters of the cuticle and the suberin layers, which protect plant surfaces. Cutinase production is typical for plant pathogenic fungi, but also, bacterial cutinases and cutinases from plant pollen have been discovered. Cutinases are promiscuous esterases catalysing reactions with a wide range of different substrates, such as short-chain soluble esters, water-insoluble medium and long-chain triacylglycerols, polyesters and waxes. In the current work, an overview is given on suggested applications of cutinases in the textile industry, in laundry detergents, in processing of biomass and food, in biocatalysis and in detoxification of environmental pollutants. The applications are discussed from the point of view of cutinase properties—which properties of cutinases are already advantageous and which would be desired. In addition, improvements that have been made on cutinase performance by protein and reaction engineering are reviewed. Springer-Verlag Berlin Heidelberg, 2015 Cutin nationallicence Suberin nationallicence Cutinase nationallicence Esterase nationallicence Applications nationallicence Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/12(2015-06-01), 4931-4942 0175-7598 99:12<4931 2015 99 253 https://doi.org/10.1007/s00253-015-6596-z text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-015-6596-z text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Nyyssölä Antti VTT Technical Research Centre of Finland Ltd., Industrial Biotechnology, P.O. Box 1000, 02044, Espoo, Finland aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/12(2015-06-01), 4931-4942 0175-7598 99:12<4931 2015 99 253