全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...

Performance Comparison of α- and β-Amylases on Chitosan Hydrolysis

DOI: 10.1155/2013/186159

Full-Text   Cite this paper   Add to My Lib

Abstract:

The low solubility in common solvent and high viscosity resulting from its high molecular weight (MW) with fiber-like structure prevents a more widespread use of chitosan. This paper presents a performance comparison of nonspecific, commercially available enzymes, α- and β-amylases, for the hydrolysis of chitosan to lower its MW. The results showed that both enzymes demonstrate the ability to be used as catalysts in chitosan hydrolysis with β-amylase having better performance than α-amylase. The chitosan hydrolysis was influenced by not only the enzyme and the chitosan characteristics but also the hydrolysis condition. The optimum pH solution was 4 for α-amylase and 5 for β-amylase. The hydrolysis temperature was found to be optimal at 90 and 50°C for α- and β-amylases, respectively. 1. Introduction Chitosan is a natural polysaccharide composed of β-(1-4) linked 2-amino-2-deoxy-D-glucopyranose and 2-acetamido-2-deoxy-D-glucopyranose, which is nontoxic, biodegradable, and biocompatible. Chitosan is commercially produced by deacetylation of chitin, which can be extracted from the exoskeleton of crustaceans (such as shrimp, lobster, crabs, and fish) and cell walls of fungi [1, 2]. Chitosan has been considered as a functional biopolymer, which is widely used in various industrial applications such as food and nutrition, medical and pharmaceutical, and cosmetic industries as well as environmental and agricultural industries [1–5]. Nevertheless, its low solubility in common solvent and high viscosity caused by its high molecular weight with fiber-like structure prevents a more widespread use of chitosan especially in food and medical applications. It was reported that low molecular weight chitosan (LMWC) that has an average molecular weight within the range 5000–10000?Da exhibits better biological activities than high molecular weight chitosan (HMWC) [4, 6]. Further, this LMWC had potential as a DNA delivery system [7]. Kondo et al. reported that LMWC with 20?kDa restricts progression of diabetes mellitus and displays higher affinity for lipopolysaccharides than 140?kDa chitosan [8]. Other studies showed that LMWC exhibits special biological and chemical activities such as antimicrobial activity [3, 9, 10], antifungal [11, 12], and antitumor activity [13, 14]. Therefore, lowering chitosan molecular weight to produce more water soluble chitosan (chitosan oligosaccharides) is gaining increased importance for broadening chitosan applications especially in food and biomedical industries. Several methods have been proposed to lower chitosan molecular weight. In

References

[1]  M. N. V. Ravi Kumar, “A review of chitin and chitosan applications,” Reactive and Functional Polymers, vol. 46, no. 1, pp. 1–27, 2000.
[2]  R. Jayakumar, D. Menon, K. Manzoor, S. V. Nair, and H. Tamura, “Biomedical applications of chitin and chitosan based nanomaterials—a short review,” Carbohydrate Polymers, vol. 82, no. 2, pp. 227–232, 2010.
[3]  S.-K. Kim and N. Rajapakse, “Enzymatic production and biological activities of chitosan oligosaccharides (COS): a review,” Carbohydrate Polymers, vol. 62, no. 4, pp. 357–368, 2005.
[4]  J. Li, Y. Du, and H. Liang, “Influence of molecular parameters on the degradation of chitosan by a commercial enzyme,” Polymer Degradation and Stability, vol. 92, no. 3, pp. 515–524, 2007.
[5]  F. Shahidi, J. K. V. Arachchi, and Y.-J. Jeon, “Food applications of chitin and chitosans,” Trends in Food Science and Technology, vol. 10, no. 2, pp. 37–51, 1999.
[6]  F. S. Kittur, A. B. Vishu Kumar, and R. N. Tharanathan, “Low molecular weight chitosans preparation by depolymerization with Aspergillus niger pectinase, and characterization,” Carbohydrate Research, vol. 338, no. 12, pp. 1283–1290, 2003.
[7]  S. C. W. Richardson, H. V. J. Kolbe, and R. Duncan, “Potential of low molecular mass chitosan as a DNA delivery system: biocompatibility, body distribution and ability to complex and protect DNA,” International Journal of Pharmaceutics, vol. 178, no. 2, pp. 231–243, 1999.
[8]  Y. Kondo, A. Nakatani, K. Hayashi, and M. Ito, “Low molecular weight chitosan prevents the progression of low dose streptozotocin-induced slowly progressive diabetes mellitus in mice,” Biological and Pharmaceutical Bulletin, vol. 23, no. 12, pp. 1458–1464, 2000.
[9]  A. B. Vishu Kumar, M. C. Varadaraj, R. G. Lalitha, and R. N. Tharanathan, “Low molecular weight chitosans: preparation with the aid of papain and characterization,” Biochimica et Biophysica Acta, vol. 1670, no. 2, pp. 137–146, 2004.
[10]  L.-Y. Zheng and J.-F. Zhu, “Study on antimicrobial activity of chitosan with different molecular weights,” Carbohydrate Polymers, vol. 54, no. 4, pp. 527–530, 2003.
[11]  B. Kang, Y.-D. Dai, H.-Q. Zhang, and D. Chen, “Synergetic degradation of chitosan with gamma radiation and hydrogen peroxide,” Polymer Degradation and Stability, vol. 92, no. 3, pp. 359–362, 2007.
[12]  Y. Xie, J. Hu, Y. Wei, and X. Hong, “Preparation of chitooligosaccharides by the enzymatic hydrolysis of chitosan,” Polymer Degradation and Stability, vol. 94, no. 10, pp. 1895–1899, 2009.
[13]  C. Q. Qin, Y. M. Du, L. Xiao, Z. Li, and X. Gao, “Enzymic preparation of water-soluble chitosan and their antitumor activity,” International Journal of Biological Macromolecules, vol. 31, no. 1–3, pp. 111–117, 2002.
[14]  W.-G. Seo, H.-O. Pae, N.-Y. Kim et al., “Synergistic cooperation between water-soluble chitosan oligomers and interferon-γ for induction of nitric oxide synthesis and tumoricidal activity in murine peritoneal macrophages,” Cancer Letters, vol. 159, no. 2, pp. 189–195, 2000.
[15]  C. T. Tsao, C. H. Chang, Y. Y. Lin, M. F. Wu, J. L. Han, and K. H. Hsieh, “Kinetic study of acid depolymerization of chitosan and effects of low molecular weight chitosan on erythrocyte rouleaux formation,” Carbohydrate Research, vol. 346, no. 1, pp. 94–102, 2011.
[16]  H.-G. Yoon, H.-Y. Kim, Y.-H. Lim et al., “Thermostable chitosanase from Bacillus sp. Strain CK4: cloning and expression of the gene and characterization of the enzyme,” Applied and Environmental Microbiology, vol. 66, no. 9, pp. 3727–3734, 2000.
[17]  T. Roncal, A. Oviedo, I. L. de Armentia, L. Fernández, and M. C. Villarán, “High yield production of monomer-free chitosan oligosaccharides by pepsin catalyzed hydrolysis of a high deacetylation degree chitosan,” Carbohydrate Research, vol. 342, no. 18, pp. 2750–2756, 2007.
[18]  C. Q. Qin, Y. M. Du, and L. Xiao, “Effect of hydrogen peroxide treatment on the molecular weight and structure of chitosan,” Polymer Degradation and Stability, vol. 76, no. 2, pp. 211–218, 2002.
[19]  S. Wu, “Preparation of water soluble chitosan by hydrolysis with commercial α-amylase containing chitosanase activity,” Food Chemistry, vol. 128, no. 3, pp. 769–772, 2011.
[20]  Y. Xie, J. Hu, Y. Wei, and X. Hong, “Preparation of chitooligosaccharides by the enzymatic hydrolysis of chitosan,” Polymer Degradation and Stability, vol. 94, no. 10, pp. 1895–1899, 2009.
[21]  M. Sardar, I. Roy, and M. N. Gupta, “A smart bioconjugate of alginate and pectinase with unusual biological activity toward chitosan,” Biotechnology Progress, vol. 19, no. 6, pp. 1654–1658, 2003.
[22]  F. A. Abd-Elmohdy, Z. El Sayed, S. Essam, and A. Hebeish, “Controlling chitosan molecular weight via bio-chitosanolysis,” Carbohydrate Polymers, vol. 82, no. 3, pp. 539–542, 2010.
[23]  H. Lin, H. Wang, C. Xue, and M. Ye, “Preparation of chitosan oligomers by immobilized papain,” Enzyme and Microbial Technology, vol. 31, no. 5, pp. 588–592, 2002.
[24]  J. Li, Y. Du, J. Yang, T. Feng, A. Li, and P. Chen, “Preparation and characterisation of low molecular weight chitosan and chito-oligomers by a commercial enzyme,” Polymer Degradation and Stability, vol. 87, no. 3, pp. 441–448, 2005.
[25]  G. Delheye and E. Moreels, “Dextrose equivalent measurements on commercial syrups,” Starch, vol. 40, pp. 430–432, 1988.
[26]  S. Sivaramakrishnan, D. Gangadharan, K. M. Nampoothiri, C. R. Soccol, and A. Pandey, “α-Amylases from microbial sources—an overview on recent developments,” Food Technology and Biotechnology, vol. 44, no. 2, pp. 173–184, 2006.

Full-Text

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133