The current study describes heterologous expression and biochemical characterization of single-modular chitinase-D from Serratia marcescens (SmChiD) with unprecedented catalytic properties which include chitobiase and transglycosylation (TG) activities besides hydrolytic activity. Without accessory domains, SmChiD, hydrolyzed insoluble polymeric chitin substrates like colloidal, alpha- and beta-chitin. Activity studies on CHOS with degree of polymerization (DP) 2-6 as substrate revealed that SmChiD hydrolyzed DP2 with a chitobiase activity and showed TG activity on CHOS with DP3-6, producing longer chain CHOS. But, the TG products were further hydrolyzed to shorter chain CHOS with DP1-2 products. SmChiD with its unique catalytic properties, could be a potential enzyme for the production of long chain CHOS and also for the preparation of efficient enzyme cocktails for chitin degradation. (C) 2016 Elsevier Ltd. All rights reserved.