Enzymatic modification of native chitin and chitin oligosaccharides by an alkaline chitin deacetylase from Microbacterium esteraromaticum MCDA02

In this study, chitin deacetylase from Microbacterium esteraromaticum MCDA02 (MeCDA) was purified ammonium sulfate precipitation, anion exchange chromatography, and superdex column chromatography. The molecular weight of purified MeCDA was approximately 26 kDa. The optimum pH and temperature of purified MeCDA were 8.0 and 30 degrees C, respectively. The enzyme activity is enhanced by metal ions K+ and Sr+ and inhibited by Co2+, Cd2+, and EDTA. The degree of deacetylation th.rough enzymatic modification of MeCDA was removed an average of 32.75% of the acetyl groups for alpha-chitin by acid-base titration. Meanwhile, MeCDA catalyze the hydrolytic cleavage of the acetamido bond in GlcNAc units within chitin oligomers and polymers. Hence, the MeCDA is a potent chitin decomposer to catalyze chitin and chitin oligosaccharides deacetylation prepare chitosan and chitosan oligosaccharide. This is a value-added utilization of chitin based biological resources.

Automated summary

In this study, chitin deacetylase from Microbacterium esteraromaticum MCDA02 (MeCDA) was purified and characterized. The enzyme can efficiently catalyze the deacetylation of chitin and hydrolytic cleavage of the acetamido bond in GlcNAc units. These findings suggest a value-added utilization of chitin based biological resources.