Kinetic Properties and Role of Bacterial Chitin Deacetylase in the Bioconversion of Chitin to Chitosan

ISSN: 2212-4012 (Online)
ISSN: 1872-2083 (Print)


Volume 10, 3 Issues, 2016


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Recent Patents on Biotechnology

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Editor-in-Chief:
Nikolaos Labrou
Laboratory of Enzyme Technology, Department of Biotechnology
Agricultural University of Athens Iera Odos 75, Gr-118 55
Athens
Greece


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Kinetic Properties and Role of Bacterial Chitin Deacetylase in the Bioconversion of Chitin to Chitosan



Recent Patents on Biotechnology, 7(3): 234-241.

Author(s): Ahmed ElMekawy, Hanaa M. Hegab, Ashraf El-Baz and Samuel M Hudson.

Affiliation: Institute of Advanced Technology & New Materials, City of Scientific Research & Technology Application Borg Elarab, Alexandria, Egypt

Abstract

Chitin is an extremely insoluble material with very limited industrial use; however it can be deacetylated to soluble chitosan which has a wide range of applications. The enzymatic deacetylation of various chitin samples was investigated using the bacterial chitin deacetylase (CDA), which was partially purified from Alcaligenes sp. ATCC 55938 growth medium and the kinetic parameters of the enzyme were determined. Also, the efficiency of biocatalyst recycling by immobilization technique was examined. CDA activity reached its maximum (0.419 U/ml) after 18 h of bacterial cultivation. When glycol chitin was used as a substrate, the optimum pH of the enzyme was estimated to be 6 after checking a pH range between 3 and 9, while the optimum temperature was found to be 35°C. Addition of acetate (100 mM) in the assay mixture resulted in 50% loss of enzyme activity. The Km value of the enzyme is 1.6 × 10-4 µ M and Vmax is 24.7 µ M/min. The average activity of CDA was 0.38 U/ml for both of immobilized and freely suspended cells after 18 h of bacterial growth. Some related patents are also discussed here.

Keywords:

Chitin deacetylase, phylogenetics, chitin, chitosan, kinetics, biopolymers, immobilization.



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Article Details

Volume: 7
Issue Number: 3
First Page: 234
Last Page: 241
Page Count: 8
DOI: 10.2174/1872208307666131202192453
Price: $100
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