Biochemical characterization of Aspergillus niger CfcI, a glycoside hydrolase family 18 chitinase that releases monomers during substrate hydrolysis

Microbiology
Jolanda M van MunsterMarc J E C van der Maarel

Abstract

The genome of the industrially important fungus Aspergillus niger encodes a large number of glycoside hydrolase family 18 members annotated as chitinases. We identified one of these putative chitinases, CfcI, as a representative of a distinct phylogenetic clade of homologous enzymes conserved in all sequenced Aspergillus species. Where the catalytic domain of more distantly related chitinases consists of a triosephosphate isomerase barrel in which a small additional (α+β) domain is inserted, CfcI-like proteins were found to have, in addition, a carbohydrate-binding module (CBM18) that is inserted in the (α+β) domain next to the substrate-binding cleft. This unusual domain structure and sequence dissimilarity to previously characterized chitinases suggest that CfcI has a novel activity or function different from chitinases investigated so far. Following its heterologous expression and purification, its biochemical characterization showed that CfcI displays optimal activity at pH 4 and 55-65 °C and degrades chitin oligosaccharides by releasing N-acetylglucosamine from the reducing end, possibly via a processive mechanism. This is the first fungal family 18 exochitinase described, to our knowledge, that exclusively releases monome...Continue Reading

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Citations

Jul 9, 2013·Microbiology·Jolanda M van MunsterMarc J E C van der Maarel
Jan 5, 2014·Fungal Genetics and Biology : FG & B·Georgios D TzelepisMagnus Karlsson
Feb 28, 2015·Carbohydrate Research·Jolanda M van MunsterMarc J E C van der Maarel
Sep 16, 2014·Applied Microbiology and Biotechnology·Jolanda M van MunsterMarc J E C van der Maarel
Feb 27, 2019·The Journal of Microbiology·Dawoon ChungJaejoon Jung
Nov 14, 2020·Molecular Biology and Evolution·Kristie D GoughenourChad A Rappleye

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