Please use this identifier to cite or link to this item: http://repository.ipb.ac.id/handle/123456789/41266
Title: Characterization of chitosanase of bacillus licheniformis mb-2 isolated from manado hot spring water
Authors: Chasanah, Ekowati
Issue Date: 2004
Publisher: IPB (Bogor Agricultural University)
Abstract: Chitosanase (EC 3.2.1.132) is an important enzyme in the production of chitosan oligomers. This research dealt with chitosanase of Indonesian origin, which was produced by chitinolytic bacteria isolated from Manado hot spring water, referred to as B. licheniformis MB-2. Specifically, the aims of the research were: (1) to produce and purify chitosanase from the bacteria, (2) analyze biochemical characteristics of the enzyme, (3) classify the enzyme based on biochemicd and preliminary bioinfmatics molecular study. The result showed that the optimum media for producing the enzyme were 0.24% chitosan, 0.25% casiton, 1% MgS04, 1.4% K2HP04, 0.02% CaC12.2H20, 0.002% FeS04.7H20. Enzyme harvested at the third day had an activity of 0.7 U/mL, while that harvested at the seventh day showed an activity of 0.8 U/mL
URI: http://repository.ipb.ac.id/handle/123456789/41266
Appears in Collections:DT - Agriculture Technology

Files in This Item:
File Description SizeFormat 
Cover_2005ech.pdf
  Restricted Access
Cover468.02 kBAdobe PDFView/Open
Bab I_2005ech.pdf
  Restricted Access
Bab I317.01 kBAdobe PDFView/Open
Bab II_2005ech.pdf
  Restricted Access
Bab II470.58 kBAdobe PDFView/Open
Bab III_2005ech.pdf
  Restricted Access
Bab III540.85 kBAdobe PDFView/Open
Bab IV_2005ech.pdf
  Restricted Access
Bab IV4.35 MBAdobe PDFView/Open
Bab V_2005ech.pdf
  Restricted Access
Bab V344.51 kBAdobe PDFView/Open
Daftar Pustaka_2005ech.pdf
  Restricted Access
Daftar Pustaka10.3 MBAdobe PDFView/Open
2004ech.pdf
  Restricted Access
Full Text19.12 MBAdobe PDFView/Open
2004ech_abstract.pdf
  Restricted Access
abstract63.35 kBAdobe PDFView/Open
2004ech_abstract.ps
  Restricted Access
abstract415.94 kBPostscriptView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.