Tekedar, H.C., Waldbieser, G.C., Kars, A., Liles, M.R., Griffin, M.J., Vamenta, S., Sonstegard, T., Hossain, M., Schroeder, S.G., Khoo, L. and Lawrence, M.L. (2013) Complete Genome Sequence of a Channel Catfish Epidemic Isolate, Aeromonas hydrophila Strain ML09-119. Genome Announcements, 1, e00755-13. http://dx.doi.org/10.1128/genomea.00755-13

has been cited by the following article:

• TITLE: Degradation of Chitin and Chitosan by a Recombinant Chitinase Derived from a Virulent Aeromonas hydrophila Isolated from Diseased Channel Catfish

  AUTHORS: Dunhua Zhang, John M. Bland, Dehai Xu, Siyin Chung

  KEYWORDS: Aeromonas hydrophila, Recombinant Chitinase, Chitin Degradation, Chitosan Degradation

  JOURNAL NAME: Advances in Microbiology, Vol.5 No.9, August 26, 2015

  ABSTRACT: A chitinase was identified in extracellular products of a virulentAeromonas hydrophilaisolated from diseased channel catfish (Ictalurus punctatus). Recombinant chitinase (rChi-Ah) was produced inEscherichia coli. Purified rChi-Ah had optimal activity at temperature of 42℃and pH 6.5. The affinity (Km) for chitosan was 4.18 mg·ml-1withVmaxof 202.5 mg·min-1·mg-1. With colloidal chitin as substrate, rChi-Ah generated N,N’-diacetyl-glucosamine predominantly. Conversion of chitosan (≥75% deacetylated) by rChi-Ah revealed five major products: 2 to 4 units of glucosamine, all of which had at least one acetyl group. It was determined that N-acetylated glucosamine was the recognition and cleavage site of rChi-Ah; the minimal and maximal cleavages were two and four glucosamine units, respectively. Functional analysis of rChi-Ah suggests thatA. hydrophilachitinase is a bioactive chitinolytic enzyme, which may benefit the pathogen for survival and/or infection.