Molecular dissection of selected chitinases and chitin binding proteins from bacterial sources

Current advances

Kaur/Appa Rao studied interaction between glycosyl hydrolase (GH) family 18 chitinases (Chi) and family 33 chitin binding proteins (CBPs) from Bacillus thuringiensis serovar kurstaki (BtChi and BtCBP), B. licheniformis DSM13 (BliChi and BliCBP) and Serratia proteamaculans 568 (SpChiB and SpCBP21). The efficiency and synergistic action of BtChi, BliChi, and SpChiB individually with BtCBP, BliCBP, or SpCBP21 was studied in detail. Chitinase assay revealed that only BtChi and SpChiB showed synergism in hydrolysis of chitin, while there was no increase in products generated by BliChi in the presence of the three above mentioned CBPs. Chitinase assay with BliGH revealed that the accessory domains play a major role in making BliChi an efficient enzyme. The BtCBP, BliCBP, or SpCBP21 did not act synergistically with chitinases in hydrolysis of the chitin, present in fungal cell walls interspersed with other polymers. Kaur published these findings in Microbiological Research in 2013. In col. with Moerschbacher, Kaur plans to characterize the binding and hydrolytic activities of CBPs and chitinase mutants and analyze the products generated by these mutants using mass spectrometry (MS) in collaboration at University of Münster (col. Mormann).

Last update 17.04.2013

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