Peripheral enzymatic deacetylation of chitin and reprecipitated chitin particles.
The enzymatic deacetylation of various chitin preparations was investigated using the fungal chitin deacetylase (CDA) isolated from Rhizopus oryzae growth medium. Specific extracellular enzyme activity after solid state fermentation was 10 times higher than that after submerged fermentation. Natural crystalline chitin is a very poor substrate for the enzyme, but showed a five-time better deacetylation after dissolution and reprecipitation. Chitin particles, enzymatically deacetylated for only 1% exhibited a strongly increased binding capacity towards ovalbumin, while maintaining the rigidity and insolubility of chitin in a moderate acidic environment. Because of the unique combination of properties, these CDA treated chitin materials were named "chit-in-osan". Chitinosan was shown to be an attractive matrix for column chromatography because no hydrogel formation was observed, that impaired the flow of eluent. Under the same conditions, partially deacetylated chitosan swelled and blocked the flow in the column.
Aye
Kyaw Nyein
KN
Bioprocess Technology, Asian Institute of Technology, P.O. Box 4, Klong Luang, Pathumthani 12120, Thailand.
Karuppuswamy
Renuka
R
Ahamed
Tangir
T
Stevens
Willem F
WF
D000581:Amidohydrolases / Q000378:metabolism*; D002686:Chitin / Q000378:metabolism*; D002845:Chromatography / Q000379:methods*; D005285:Fermentation; D010047:Ovalbumin / Q000378:metabolism; D012233:Rhizopus / Q000201:enzymology
D002686:Chitin; D010047:Ovalbumin; D000581:Amidohydrolases; C019866:chitin deacetylase