| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7086978 | Bioresource Technology | 2012 | 9 Pages |
Abstract
⺠Cloning and characterization of three chitinases from Serratia proteamaculans 568. ⺠All three Sp chitinases displayed highest activity/binding to β-chitin. ⺠Released dimer as major end product from oligomeric and polymeric substrates. ⺠The three Sp chitinases are endo-enzymes released up to tetramers from polymer. ⺠Sp ChiA and Sp ChiB were processive, while Sp ChiC was non-processive.
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Authors
Pallinti Purushotham, P.V.S.R.N. Sarma, Appa Rao Podile,