Activation of enzymatic chitin degradation by a lytic polysaccharide monooxygenase
| Autor: | Morten Sørlie, Anne Grethe Hamre, Kristine Bistrup Eide, Hanne H. Wold |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
chemistry.chemical_classification
biology Hydrolysis Chitinases Organic Chemistry Chitin General Medicine Monooxygenase biology.organism_classification Polysaccharide Biochemistry Mixed Function Oxygenases Substrate Specificity Analytical Chemistry chemistry.chemical_compound Enzyme Bacterial Proteins chemistry Serratia marcescens Glycoside hydrolase Cellulose |
| Zdroj: | Carbohydrate Research. 407:166-169 |
| ISSN: | 0008-6215 |
| Popis: | For decades, the enzymatic conversion of recalcitrant polysaccharides such as cellulose and chitin was thought to solely rely on the synergistic action of hydrolytic enzymes, but recent work has shown that lytic polysaccharide monooxygenases (LPMOs) are important contributors to this process. Here, we have examined the initial rate enhancement an LPMO (CBP21) has on the hydrolytic enzymes (ChiA, ChiB, and ChiC) of the chitinolytic machinery of Serratia marcescens through determinations of apparent k(cat) (k(cat)(app)) values on a β-chitin substrate. k(cat)(app) values were determined to be 1.7±0.1 s(-1) and 1.7±0.1 s(-1) for the exo-active ChiA and ChiB, respectively and 1.2±0.1 s(-1) for the endo-active ChiC. The addition of CBP21 boosted the k(cat)(app) values of ChiA and ChiB giving values of 11.1±1.5 s(-1) and 13.9±1.4 s(-1), while there was no effect on ChiC (0.9±0.1 s(-1)). |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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