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The aim of this work was the application of purified chitinolytic enzyme from Cellulosimicrobium cellulans 191 and the commercial papain in the hydrolysis of colloidal chitin. The latter was characterized with regard to the degree deacetylation (GD), with a GD of 14% being obtained using infrared spectroscopy. The purified chitinase hydrolysed the colloidal chitin and formed di-N-acetylchitobiose, while the commercial papain acting on the same substrate formed di-N-acetylchitobiose and tri-N-acetylchitotriose. The aminoglucanoligosaccharides chemical structure was elucidated by mass spectrometry.O presente trabalho visou a aplicação da enzima quitinolítica purificada da linhagem Cellulosimicrobium cellulans 191 e da preparação comercial de papaína na hidrólise da quitina coloidal. A quitina coloidal foi caracterizada quanto ao grau de desacetilação e apresentou GD de 14% por espectroscopia na região do infravermelho. A quitinase purificada hidrolisou a quitina coloidal liberando di-N-acetilquitobiose, enquanto que a preparação comercial de papaína atuando sobre o mesmo substrato formou di-N-acetilquitobiose e tri-N-acetilquitotriose. A estrutura química dos aminoglucanooligossacarídeos foi elucidada por espectrometria de massa

Elucidação parcial da estrutura de aminoglucanooligossacarídeos (AGO's) produzidos enzimaticamente