TAILIEUCHUNG - Báo cáo khoa học: The chitinolytic system of Lactococcus lactis ssp. lactis comprises a nonprocessive chitinase and a chitin-binding protein that promotes the degradation of a- and b-chitin

It has recently been shown that the Gram-negative bacterium Serratia marcescensproduces an accessory nonhydrolytic chitin-binding protein that acts in synergy with chitinases. This provided the first example of the pro-duction of dedicated helper proteins for the turnover of recalcitrant polysaccharides. | The chitinolytic system of Lactococcus lactis ssp. lactis comprises a nonprocessive chitinase and a chitin-binding protein that promotes the degradation of a- and b-chitin Gustav Vaaje-Kolstad Anne C. Bun s Geir Mathiesen and Vincent G. H. Eijsink Department of Chemistry Biotechnology and Food Science Norwegian University of Life Sciences As Norway Keywords chitin chitin binding chitinase lactic acid bacterium Lactococcus lactis Correspondence G. Vaaje-Kolstad Department of Chemistry Biotechnology and Food Science Norwegian University of Life Sciences PO Box 5003 1432 As Norway Fax 47 64965901 Tel 47 64965905 E-mail Received 23 December 2008 revised 10 February 2009 accepted 18 February 2009 doi It has recently been shown that the Gram-negative bacterium Serratia marcescens produces an accessory nonhydrolytic chitin-binding protein that acts in synergy with chitinases. This provided the first example of the production of dedicated helper proteins for the turnover of recalcitrant polysaccharides. Chitin-binding proteins belong to family 33 of the carbohydrate-binding modules and genes putatively encoding these proteins occur in many microorganisms. To obtain an impression of the functional conservation of these proteins we studied the chitinolytic system of the Gram-positive Lactococcus lactis ssp. lactis IL1403. The genome of this lactic acid bacterium harbours a simple chitinolytic machinery consisting of one family 18 chitinase named LlChi18A one family 33 chitin-binding protein named LICBP33A and one family 20 N-acetylhexosaminidase. We cloned overexpressed and characterized LlChi18A and LlCBP33A. Sequence alignments and structural modelling indicated that LlChi18A has a shallow substrate-binding groove characteristic of nonprocessive endochitinases. Enzymology showed that LlChi18A was able to hydrolyse both chitin oligomers and artificial substrates with no sign of processivity. Although the .

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