Journal of
Agricultural Biotechnology and Sustainable Development

  • Abbreviation: J. Agric. Biotech. Sustain. Dev.
  • Language: English
  • ISSN: 2141-2340
  • DOI: 10.5897/JABSD
  • Start Year: 2009
  • Published Articles: 120

Full Length Research Paper

Modification of surface structure and crystallinity of water hyacinth (Eichhornia crassipes) following recombinant α-L-arabinofuranosidase (abfa) treatment

Anita Kurniati1, Handoko Darmokoesoemo2 and N. N. T. Puspaningsih1,2*
  1Proteomic Laboratory, Institute of Tropical Disease, Airlangga University, Campus C Mulyorejo, Surabaya, East Java 60115, Indonesia. 2Department of Chemistry, Faculty of Science and Technology, Airlangga University, Campus C Mulyorejo, Surabaya, East Java 60115, Indonesia.
Email: [email protected]

  • Article Number - 0C99BDA1770
  • Vol.3(9), pp. 182-188, November 2011
  •  Accepted: 06 September 2011
  •  Published: 30 November 2011

Abstract

 

This research was aimed to investigate the modification of surface structure and crystallinity of water hyacinth after recombinant α-L-arabinofuranosidase treatment. The process of water hyacinth hydrolysis was optimized first, by determination of the most optimal intracellular enzyme (P) and extracellular enzyme (S) mixture ratio, and its incubation time. The optimum of water hyacinth hydrolysis process was achieved at ratio P:S = 1:2, after 8 h incubation. The surface structure of water hyacinth after recombinant α-L-arabinofuranosidase treatment was analyzed by scanning electron microscope (SEM) and X-ray diffraction (XRD), using untreated water hyacinth as control. This research showed that enzymatic hydrolysis damaged the surface structure of water hyacinth and changed its crystallinity. The enzyme used in this research can be applied further for bio-bleaching of paper pulp and animal feed stock, while the hydrolysis product can be applied for bioethanol production.  

 

Key words: Water hyacinth, α-L-arabinofuranosidase, scanning electron microscope, X-ray diffraction.

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