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KMID : 0545120000100060805
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Journal of Microbiology and Biotechnology
2000 Volume.10 No. 6 p.805 ~ p.810
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Purification and Characterization of a Novel Antifungal Protein from Paenibacillus macerans PM1 Antagonistic to Rice Blast Fungus,Pyricularia oryzae
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Bae, Dong Won
Kawk, Yeong Sik/Lee, Joon Taek/Son, Dae Young/Chun, Sung Sik/Kim, Hee Kyu
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Abstract
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An antifungal protein antagonistic to the rice blast fungus, Pyricularia oryzae was purified from Paenibacillus macerans PM-1 by ammonium sulfate fractionation, Q Sepharose Fast Flow column chromatography, Phenyl Sepharose CL-4B column chromatography and Superose 12gel filtration. An apparent molecular mass of the purified antifungal protein was determined as 8kDa by SDS-PAGE and 9kDa by analytical gel filtration, respectively, suggesting that the purified protein is a monomer. The antifungal protein was stable at pH range from 7-12 and up to 100℃. The protein was also stable at 0.1-1% Tween 20 and Triton X-100. The N-terminal amino acid sequence of the antifungal protein was Thr-Glu-Leu-Pro-Leu-Gly-Ile-Val-Met-Asp-Lys-Tyr-Thr-Asp-Ala-Phe-Lys-Phe-Asp-Met-Phe. Comparison of the determined sequence with other peptide and DNA sequences did not reveal homology at all. Therefore, the purified antifungal protein was speculated to be a novel protein. The conidial germination in vitro of P oryzae KJ 301: 93-39 by the purified protein (5.9㎍/㎖) was limited to 9±3.2% only, compared with 69±2.4% of the control. Ungerminated conidia were swollen at basal and mid cell by the purified protein. In vivo bioassay for inhibition of conidial germination of P oryzae KJ 301, one of the most predominating races in Korea, the purified protein (5.9㎍/㎖) strongly inhibited the conidial germination. The conidia, even though germinated, could not develop any further to produce appressoria efficiently.
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