[P007] Poster

12:10 PM - 1:00 PM JST(3:10 AM - 4:00 AM UTC)

[P04-535] C-terminal Truncation of Chitinase Cq181 Enhances
Catalytic Performance and Diversifies Oligosaccharide Products

○Ying Zhou¹, Yujiao Li¹ (1. Harbin Institute of Technology, Weihai (China))

Keywords:

chitinase,domain truncation,C-terminal domain,product profile

The catalytic function of chitinases is closely associated with their multi-domain structure. This study aims to clarify the specific contributions of individual domains to enzyme activity, thermostability, and product distribution. We investigated chitinase Cq181 from the marine bacterium Aeromonas sp. RPC2, which consists of an N-terminal chitin-binding domain, a catalytic domain, and a functionally uncharacterized C-terminal non-catalytic domain. Truncated variants were constructed, and removal of the C-terminal non-catalytic domain in the variant Cq181NC resulted in a specific activity of 440.17 U/mg, a 1.8-fold increase over the wild-type, and enhanced its thermostability at 35°C to 1.43 times that of the wild-type. Notably, the product profile also shifted: while the wild-type Cq181 predominantly generated disaccharide, consistent with an exo-chitinase activity, the Cq181NC variant produced a diverse mixture of oligosaccharides, including mono-, di-, tri-, and hexasaccharides. These findings demonstrate that the C-terminal non-catalytic domain plays a critical role in modulating the catalytic performance, thermal stability, and product composition of Cq181, offering important insights for the rational design of high-efficiency chitinases.