Biochemical Studies

Enzymatic Depolymerization of N-Succinylchitosan

A. V. Il’ina1 and V. P. Varlamov1#

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1Center of Bioengineering, Russian Academy of Sciences, pr. 60-letiya Oktyabrya 7, k. 1, Moscow, 117312, Russia

Received: July 15, 2006; in final form: August 4, 2006

Abstract. A complex of chitinolytic enzymes of Streptomyces kurssanovii and also lysozyme and Celloviridin, an industrial cellulase preparation, were demonstrated to provide for an enzymatic hydrolysis of N-succinylchitosan. Our studies were carried out on a high-molecular N-succinylchitosan with M of 390 kDa and a substitution degree of 0.8 as a substrate. All the enzymatic preparations were shown to be suitable for the obtaining of low-molecular derivatives of N-succinylchitosan. The complex of enzymes from S. kurssanovii showed the greatest activity: they reduced the characteristic viscosity of initial solution of the substrate by 78% for 30 min. A biodegradation of N-succinylchitosan of various molecular masses was shown to proceed under the action of lysozyme, and the cleavage reaction was revealed to decelerate at a decrease of the polymer molecular mass. A use of N-succinylchitosan in a complex with drugs for a prolongation of their action in a live organism was presumed.

Key words: chitin, chitinaseschitosanlysozyme, N-succinylchitosan, enzymatic depolymerization, biodegradation

Russian Journal of Bioorganic Chemistry 2007, 33 (1): 146-149