Insect-Derived Chitinases

Autor(en): Merzendorfer, Hans 
Herausgeber: Vilcinskas, A
Stichwörter: BACILLUS-THURINGIENSIS; BETA-N-ACETYLGLUCOSAMINIDASE; Biopesticides; Biotechnology & Applied Microbiology; Carbohydrate binding module 14; CBM14; Chitin binding domain; Engineering; Engineering, Biomedical; Engineering, Chemical; FAMILY 18 CHITINASES; Family 18 glycoside hydrolase; GH18 domain; Insect chitinase; LARVAL PUPAL TRANSFORMATION; MANDUCA-SEXTA-CHITINASE; MOLECULAR CHARACTERIZATION; PERITROPHIC MATRIX; Pest control; PLASMODIUM-FALCIPARUM CHITINASE; TICK HAEMAPHYSALIS-LONGICORNIS; VIRUS-ENCODED CHITINASE
Erscheinungsdatum: 2013
Herausgeber: SPRINGER-VERLAG BERLIN
Journal: YELLOW BIOTECHNOLOGY II: INSECT BIOTECHNOLOGY IN PLANT PROTECTION AND INDUSTRY
Advances in Biochemical Engineering-Biotechnology
Volumen: 136
Startseite: 19
Seitenende: 50
Zusammenfassung: 
Insect chitinases belong to family 18 of the glycoside hydrolase superfamily (GH18) and comprise endo-splitting enzymes that retain the anomeric beta-(1,4) configuration of the cleavage products. However, some of them have lost their catalytic activity but retained the chitin binding activity and/or possess imaginal disc growth factor activity. In all sequenced insect genomes, multiple genes encode chitinases, which are differentially expressed during development and in various insect tissues. Some of them have nonredundant functions and are essential for growth and development. A characteristic property is their multidomain architecture, which comprises varying numbers of catalytic and chitinbinding domains that are connected by glycosylated serine/threonine linker regions. Based on sequence similarities and domain organization, they have been classified into eight different groups. Insect chitinases have gained increasing interest for use in the biological control of parasites, fungi, and insect pests, and some enzymes have properties that make them highly attractive for biotechnological applications.
ISBN: 9783642399022
9783642399015
ISSN: 07246145
DOI: 10.1007/10_2013_207

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