Preparation of N-acetyl-D-Glucosamine Using Enzyme from Aspergillus sp.
Keywords:
chitosan, fungi, food supplement, glucosamine, monosaccharide, sugarAbstract
N-acetyl-D-glucosamine (GlcNAc) is one of the basic constituents of mammal cartilage, which is known to help repair deteriorating cartilage and relieve pain and inflammation in osteoarthritis patients. The preparation of GlcNAc from squid pen β-chitin by using Aspergillus sp. chitinase in enzymatic hydrolysis is studied. The cultivation of the fungus in colloidal chitin minimum media at pH 3.5 and 40°C for 5 days gives the highest chitinolytic activity of 3.1 U/mL. The crude enzyme obtained from the the cultivation is used in the hydrolysis of milled squid pen β-chitin (50μm) at pH 4 (acetic acid 2M) and 45°C using 22 U of enzyme per gram of chitin. After 2 days of hydrolysis, GlcNAc is isolated in 65% yield by precipitation in ethanol from a charcoal decolorized aqueous solution.Downloads
References
Paraman, I., San, H., Chuen-How, N., Trang, S. T. and Willem, F. S. 2006. Production of N-acetyl chitobiose from various chitin substrates using commercial enzymes. Carbohydr. Polymer. 63 : 245–250.
Hitoshi, S., Shizu, F., Naoko, Y., Norioki, K., Atsuyoshi, N., Einosuke, M., Kazumi, H., Kohei, O. and Sei-ichi, A. 2002. Production of N-acetyl-D-glucosamine from α-chitin by crude enzymes from Aeromonas hydrophila H-2330. Carbohydr. Res. 337 : 761–763.
Rath, P., Sanya, K., Kamontip, K., Mongkol, S. and Sei-ichi, A. 2002. Quantitative production of 2-acetamido-2-deoxy-D-glucose from crystalline chitin by bacterial chitinase. Carbohydr. Res. 337 : 557–559.
Yuji, H., Hajime, T. and Motomitsu, K. 2008. A reducing-end-acting chitinase from Vibrio proteolyticus belonging to glycoside hydrolase family 19. Appl. Microbiol. Biotechnol. 78 : 627–634.
Li, D. C. 2006. Review of fungal chitinases. Mycopathologia. 161: 345–360.
Eddie, E. D., John, M. W., James, M. L. and John, F. P. 1998. The purification and characterization of a Trichoderma harzianum exochitinase. Biochim. Biophys. Acta 1383 : 1998.101–110.
Yong-Seok, L., In-Hye, P., Ju-Soon, Y., Soo-Yeol, C., Young-Choon, L., Young-Su, C., SoonCheol, A., Cheol-Min, K., Yong-Lark, C. 2007. Cloning, purification, and characterization of chitinase from Bacillus sp. DAU101. Bioresour. Technol. 98 : 2734–2741.
Xia, G., Jin, C., Zhou, J., Yang, S., Zhang, S. and Jin, C. 2001. A novel chitinase having a unique mode of action from Aspergillus fumigatus YJ-407. Eur. J. Biochem. 268 : 4079-4085.
Svein, J. H., Horn, S. J. and Eijsink, V.G.H. 2004. A reliable reducing end assay for chitooligosaccharides. Carbohydr. Polym. 56 : 35–39.
Ju, H. K., Woo, J. J., Gyung, H. J., Joon, S. A., Kil, Y. K. and Ro, D. P. 2004. Selective preparation of N-acetyl-D-glucosamine and N,N’-diacetylchitobiose from chitin using a crude enzyme preparation from Aeromonas sp. Biotechnol. Lett. 27 : 7-11.
Maria, S. B., Elżbieta, L. P., Wojciech, D. 2007. Chitinolytic activity of bacteria and fungi isolated from shrimp exoskeletons. Int. J. Oceanography Hydrobiol. 36(3) : 101-111.
Jana, D., Dirk, S., Zdenka, H., Joachim, T., Vladimir, K. 2001. Enzymatic rearrangement of chitin hydrolysates with β-N-acetylhexosaminidase from Aspergillus oryzae. J. Molecular. Catalysis B : Enzymatic 11 : 225–232.
Neetu, D., Rupinder, T.,Gurinder, S. H. 2006. Biotechnological aspects of chitinolytic enzymes: a review. Appl. Microbiol. Biotechnol. 71 : 773–782.
Parameswaran, B., Chandran, S., Pradeep, S., George, S., Ashok, P. 2007. Fungal biosynthesis of endochitinase and chitobiase in solid state fermentation and their application for the production of N-acetyl-Dglucosamine from colloidal chitin. Bioresour. Technol. 98 : 2742–2748.
Massimiliano, F., Roberta, D. G., Eric, R., JeanLouis L., Federico, F. 1998. Repeated-batch and continuous production of chitinolytic enzymes by Penicillium janthinellum immobilised on chemically-modified macroporous cellulose. J. Biotechnol. 62 : 119–131.
Downloads
Published
How to Cite
Issue
Section
License
Copyright (c) 2017 Journal of Metals, Materials and Minerals
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
Authors who publish in this journal agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgment of the work's authorship and initial publication in this journal.
- Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgment of its initial publication in this journal.