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Purification and Chitinolytic Characteristics of Chitinases A and B from Serratia marcescens

Jamil A. Baban1,2

1Faculty of Medical Sciences, University of Sulaimani, Sulaimaniyha, Kurdistan Region-Iraq

Correspondence: jamil.baban@univsul.edu.iq

2Norwegian University of Life Sciences, P.O. Box 5003, N-1432 Aas, Norway.



Original: 21.09.2015Revised: 21.02.2016Accepted: 21.04.2016Published online: 20.09.2016


DOI Link: 

ABSTRACT

In Serratia marcescens the enzymatic chitinolytic machinery of is one of the best that can convert insoluble polysaccharides. This process includes four chitin-active enzymes: ChiA, ChiB and ChiC, an endo-acting non-processive chitinase, , two processive chitinases moving along chitin chains in opposite directions. Serratia marcescens as a Gram-negative soil bacterium produces these three chitinases, ChiA, ChiB and ChiC which together enable Serratia marcescens to perfectly degrade the insoluble chitin polymer. The data collected for the pseudotrisaccharide allosamidin shows a comparative inhibition including the cyclic pentapeptide argadin. ChiA, ChiB and ChiC play different roles during chitin degradation was confirmed by the synergistic effects that were observed for certain combinations of ChiA, ChiB and ChiC.


 


KEYWORDS

Allosamidin, Chitin, CBP21, Isothermal Titration, Calorimetry, Chitinases, E. coli, harbouring plasmid




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