Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2017 Mar 9:10:59.
doi: 10.1186/s13068-017-0740-1. eCollection 2017.

Novel Acinetobacter parvus HANDI 309 microbial biomass for the production of N-acetyl-β-d-glucosamine (GlcNAc) using swollen chitin substrate in submerged fermentation

Tae Il Kim #  1 , Kwang Seok Ki  1 , Dong Hyun Lim  1 , Mayakrishnan Vijayakumar #  1 , Seong Min Park  1 , Sun Ho Choi  1 , Ki Young Kim  2 , Seok Ki Im  1 , Beom Young Park  1
Affiliations

Novel Acinetobacter parvus HANDI 309 microbial biomass for the production of N-acetyl-β-d-glucosamine (GlcNAc) using swollen chitin substrate in submerged fermentation

Tae Il Kim et al. Biotechnol Biofuels. .

Abstract

Background: N-acetyl-β-d-glucosamine (GlcNAc)6 is extensively used as an important bio-agent and a functional food additive. The traditional chemical process for GlcNAc production has some problems such as high production cost, low yield, and acidic pollution. Therefore, to discover a novel chitinase that is suitable for bioconversion of chitin to GlcNAc would be of great value.

Results: Here, we describe the complete isolation and functional characterization of a novel exo-chitinase from Acinetobacter parvus HANDI 309 for the conversion of chitin. The identified exo-chitinase mainly produced N-acetyl-d-glucosamine, using chitin as a substrate by submerged fermentation. The A. parvus HANDI 309 biofuels producing exo-chitinase were characterized by TLC, and was further validated and quantified by HPLC. Furthermore, the optimal temperature and pH for the exo-chitinase activity was obtained in the culture conditions of 30 °C and 7.0, respectively. The maximum growth of the stationary phase was reached in 24 h after incubation. These results suggest that A. parvus HANDI 309 biofuels producing exo-chitinases may have great potential in chitin to N-acetyl-d-glucosamine conversion.

Conclusions: The excellent thermostability and hydrolytic properties may give the exo-chitinase great potential in chitin to GlcNAc conversion in industry. This is the first report that A. parvus HANDI 309 is a novel bacterial strain that has the ability to produce an enormous amount of exo-chitinase-producing bio-agents in a short time on an industrial scale without any pretreatment, as well as being potentially valuable in the food and pharmaceutical industries.

Keywords: Acinetobacter parvus; Calves; Chitin; Chitinase; Feces; N-acetyl-d-glucosamine.

PubMed Disclaimer

Figures

Fig. 1
Fig. 1
Screening of chitinolytic activity of isolated extracellular chitinase on agar medium containing chitin and stained with Congo red
Fig. 2
Fig. 2
TLC (a) and HPLC profile (b) analysis of hydrolytic products of chitin oligosaccharides in the presence of Acinetobacter parvus HANDI 309 extracellular chitinase
Fig. 3
Fig. 3
Effect of the cell growth (a) incubation temperature (b), time (c) and pH (d) of the culture medium on A. parvus HANDI 309-produced exo-chitinase activity
Fig. 4
Fig. 4
Effect of the carbon (a), organic (b), inorganic nitrogen (c) and mineral (d) sources of the culture medium on A. parvus HANDI 309-produced exo-chitinase activity
See this image and copyright information in PMC

References

    1. Khoushab Y, Yamabhai M. Chitin research revisited. Mar Drug. 2010;8:1988–2012. doi: 10.3390/md8071988. - DOI - PMC - PubMed
    1. Dahiya N, Tewari R, Hoondal GS. Biotechnological aspects of chitinolytic enzyme: a review. Appl Microbiol Biotechnol. 2006;71:773–782. doi: 10.1007/s00253-005-0183-7. - DOI - PubMed
    1. Gohel V, Singh A, Vimal M, Ashwini P, Chhatpar HS. Review-bioprospecting and antifungal potential of chitinolytic microorganisms. Afr J Biotechnol. 2006;5:54–72.
    1. Liang TW, Chen YJ, Yen YH, Wang SL. The antitumor activity of the hydrolyzates of chitinous materials hydrolyzed by crude enzyme from Bacillus amyloliquefaciens V656. Proc Biochem. 2007;42:527–534. doi: 10.1016/j.procbio.2006.10.005. - DOI
    1. Duo-Chuan L. Review of fungal chitinases. Mycopathologia. 2006;161:345–360. doi: 10.1007/s11046-006-0024-y. - DOI - PubMed

LinkOut - more resources