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• W2034283607 abstract "ABSTRACT We purified and characterized a chitinase from the digestive gland of the white shrimp, Litopenaeus vannamei. The enzyme has a molecular mass of 50 kDa and a pI of 4.7, similar to the values calculated from the cDNA-deduced amino acid sequence. L. vannamei chitinase was stable at pH 5.0 to 8.0 and NaCl concentrations of 0–1 M, presenting an acidic pH-optimum (pH 5.5–6.0) and maximum activity at 0.45–0.6 M NaCl. Steady-state kinetics was obtained using the fluorescent substrate analog 4-methylumbelliferyll-β-D-N,N′N″-triacetylchitotrioside. The Michaelis-Menten constant was Km = 165 µM and Vmax = 0.59 µmol/min/mL at pH 6.0 and 25C, with a marginal effect of NaCl concentration on the kinetic parameters. Its molecular mass and isoelectric point indicate similarity to chitinase 3 from Penaeus japonicus. Molecular modeling revealed the presence of a hydrophobic cavity at the substrate binding site. The mRNA was detected through reverse transcription-polymerase chain reaction in the digestive gland but not in muscle, pleopods or gills, suggesting a role in food digestion. PRACTICAL APPLICATIONS The shrimp processing industry generates large amounts of shell and heads waste. Shells are chemically treated, requiring hard acid and alkali, to obtain chitosan. Shrimp heads waste also contains a large amount of hydrolytic enzymes, such as proteases and chitinases. We characterized the kinetics and the expression of a shrimp chitinase. This enzyme can be obtained as a subproduct from heads waste or produced as recombinant protein, since the cDNA sequence is available, to be used potentially for less-contaminating chitosan production." @default.
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• W2034283607 date "2009-04-01" @default.
• W2034283607 modified "2023-09-24" @default.
• W2034283607 title "KINETIC CHARACTERIZATION, EXPRESSION AND MOLECULAR MODELING OF A CHITINASE FROM THE PACIFIC WHITE SHRIMP<i>LITOPENAEUS VANNAMEI</i>" @default.
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• W2034283607 doi "https://doi.org/10.1111/j.1745-4514.2009.00215.x" @default.
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