Planta Med 2003; 69(9): 809-813
DOI: 10.1055/s-2003-43216
Original Paper
Physiology
© Georg Thieme Verlag Stuttgart · New York

Mollisin, an Antifungal Protein from the Chestnut Castanea mollissima

K. T. Chu1 , T. B. Ng1
  • 1Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China
Further Information

Publication History

Received: January 13, 2003

Accepted: April 12, 2003

Publication Date:
04 November 2003 (online)

Abstract

The isolation of a protein designated mollisin, with an N-terminal sequence manifesting some similarity to thaumatin-like proteins (TLPs), and possessing a molecular mass of 28 kDa which is higher than those of TLPs, is reported herein from the seeds of the chestnut Castanea mollisima. The protein was unadsorbed on DEAE-cellulose, and adsorbed on Affi-gel blue gel and Mono S. Mollisin exhibited a molecular mass of 28 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis as well as in gel filtration on Superdex 75 by fast protein liquid chromatography. The protein inhibited mycelial growth in Fusarium oxysporum, Mycosphaerella arachidicola and Physalospora piricola, with an IC50 of 0.83 μM, 6.48 μM and 9.21 μM, respectively. Mollisin displayed a higher antifungal potency than French bean and kiwi fruit TLPs toward F. oxysporum and M. arachidicola. The antifungal activity of mollisin was unaffected by incubation at 40 °C for 10 minutes, underwent a decline after incubation at 60 °C, and was completely abolished after treatment at 80 °C. Mollisin exhibited a more potent inhibitory activity on HIV-1 reverse transcriptase than kiwi fruit TLP.

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T. B. Ng

Department of Biochemistry

Faculty of Medicine

The Chinese University of Hong Kong

Shatin

New Territories

Hong Kong

P. R. China

Fax: +852-2603-5123

Phone: +852-2609-6875

Email: biochemistry@cuhk.edu.hk

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