2000
DOI: 10.1023/a:1007147214796
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Analysis of Essential Leucine Residue for Catalytic Activity of Novel Thermostable Chitosanase by Site-Directed Mutagenesis

Abstract: Bacterial chitosanases share weak amino acid sequence similarities at certain regions of each enzyme. These regions have been assumed to be important for catalytic activities of the enzyme. To verify this assumption, the functional importance of the conserved region in a novel thermostable chitosanase (TCH-2) from Bacillus coagulans CK108 was investigated. Each of the conserved amino acid residues (Leu64, Glu80, Glu94, Asp98, and Gly108) was changed to aspartate and glutamine or asparagine and glutamate by sit… Show more

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Cited by 5 publications
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“…First, they are highly stable in most cases since dendrimers molecules are strongly adsorbed to the initial surface in contrast to the monopodal attachment of linear alkylbased self-assembled monolayers. Moreover, since such molecules contain a large number of peripheral reactive groups as well as a structure that is molecularly controllable (type of core, the choice of branch point, and distance between successive branch junctions), they turned out to be very efficient in influencing the self-assembly properties of biomolecules [11] such as antibodies or plasmids.…”
Section: Dendrimeric Patterned Surfacesmentioning
confidence: 99%
“…First, they are highly stable in most cases since dendrimers molecules are strongly adsorbed to the initial surface in contrast to the monopodal attachment of linear alkylbased self-assembled monolayers. Moreover, since such molecules contain a large number of peripheral reactive groups as well as a structure that is molecularly controllable (type of core, the choice of branch point, and distance between successive branch junctions), they turned out to be very efficient in influencing the self-assembly properties of biomolecules [11] such as antibodies or plasmids.…”
Section: Dendrimeric Patterned Surfacesmentioning
confidence: 99%