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Exo-β-1,3-Glucanase from Yeast Inhibits Colletotrichum lupini and Botrytis cinerea Spore Germination
Authors:Dean  Oelofse  Ian  Dubery and Dave K  Berger
Institution:Authors' addresses: Agricultural Research Council, Vegetable and Ornamental Plant Institute (ARC-VOPI), Biotechnology Division, Private Bag X293, Pretoria, 0001, South Africa;;Department of Biochemistry, University of Johannesburg, PO Box 524, Auckland Park, 2006, South Africa;;Department of Plant Science, Forestry and Agricultural Biotechnology Institute (FABI), University of Pretoria, Pretoria, South Africa (correspondence to Dean Oelofse. E-mail: )
Abstract:Yeast exo-β-1,3-glucanase (EXG1) was evaluated as an inhibitory agent of Colletotrichum lupini and Botrytis cinerea. Extracts obtained from yeast transformed with the exg1 gene, expressing high levels of EXG1 activity, or control untransformed yeast cultures that lacked EXG1 activity, were added to different starting concentrations of C. lupini fungal spore suspensions (2.5 × 103 to 80 × 103 spores per flask), and mycelial dry weight was measured after 5 days. Inhibition of C. lupini mycelial growth by EXG1 compared with control extracts ranged from 41 to 20% when added to starting fungal spore concentrations of 2.5 × 103 to 80 × 103, respectively. EXG1 activity in the extracts from the transformed yeast remained high over the 5-day incubation period. Addition of the EXG1 extract after C. lupini spore germination resulted in lower inhibition, indicating that the EXG1 targets the β-glucan in the cell walls of the fungal spores at an early stage of germination. Furthermore, the yeast EXG1 extracts were also shown to inhibit Botrytis cinerea spore germination and growth. Thus, the use of the yeast exg1 gene for protection of crops, such as lupin and pear in transgenic strategies against C. lupini and B. cinerea , respectively, could be considered.
Keywords:Colletotrichum lupini                        Botrytis cinerea            anti-fungal  exo-β-1  3-glucanase              Saccharomyces cerevisiae
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