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.
Key words
Chestnut -
Castanea mollissima
- Fagaceae - thaumatin-like protein - antifungal protein
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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