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Hossain, M.J., Waldbieser, G.C., Sun, D., Capps, N.K., Hemstreet, W.B., Carlisle, K., Griffin, M.J., Khoo, L., Goodwin, A.E, Sonstegard, T,S., Schroeder, S., Hayden, K., Newton, J.C., Terhune, J.S. and Liles, M.R. (2013) Implication of Lateral Genetic Transfer in the Emergence of Aeromonas hydrophila Isolates of Epidemic Outbreaks in Channel Catfish. PLoS ONE, 8, e80943. http://dx.doi.org/10.1371/journal.pone.0080943

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.