Kunitz-Type Serine Protease Inhibitor from Potato (Solanum tuberosum L. cv. Jopung)

An antifungal protein, AFP-J, was purified from tubers of the potato (Solanum tuberosum cv. L Jopung) by various chromatographic columns. AFP-J strongly inhibited yeast fungal strains, including Candida albicans, Trichosporon beigelii, and Saccharomyces cerevisiae, whereas it exhibited no activity a...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2005-08, Vol.53 (16), p.6491-6496
Main Authors: Park, Yoonkyung, Choi, Bo Hwa, Kwak, Ji-Sun, Kang, Chang-Won, Lim, Hak-Tae, Cheong, Hyeon-Sook, Hahm, Kyung-Soo
Format: Article
Language:English
Subjects:
Amino Acid Sequence
amino acid sequences
animal pathogenic fungi
Antifungal Agents - pharmacology
antifungal properties
antimicrobial agents
Candida albicans
enzyme inhibition
Fungi - drug effects
Humans
Molecular Sequence Data
Peptides - chemistry
Peptides - isolation & purification
Peptides - pharmacology
plant proteins
Plant Proteins - chemistry
Plant Proteins - isolation & purification
Plant Proteins - pharmacology
Plant Tubers - chemistry
Plants - microbiology
potatoes
proteinase inhibitors
Saccharomyces cerevisiae
Solanum - chemistry
Solanum tuberosum
Trichosporon beigelii
tubers
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Summary:An antifungal protein, AFP-J, was purified from tubers of the potato (Solanum tuberosum cv. L Jopung) by various chromatographic columns. AFP-J strongly inhibited yeast fungal strains, including Candida albicans, Trichosporon beigelii, and Saccharomyces cerevisiae, whereas it exhibited no activity against crop fungal pathogens. Automated Edman degradation determined the partial N-terminal sequence of AFP-J to be NH2-Leu-Pro-Ser-Asp-Ala-Thr-Leu-Val-Leu-Asp-Gln-Thr-Gly-Lys-G lu-Leu-Asp-Ala-Arg-Leu-. The partially sequence had 83% homology with a serine protease inhibitor belonging to the Kunitz family, and the protein inhibited chymotrypsin, pepsin, and trypsin. Mass spectrometry showed that its molecular mass was 13 500.5 Da. This protease inhibitor suppressed over 50% the proteolytic activity at 400 μg/mL. These results suggest that AFP-J is an excellent candidate as a lead compound for the development of novel antiinfective agents. Keywords: Antifungal protein J (AFP-J); potato; serine protease inhibitor; Kunitz family
ISSN:0021-8561
1520-5118
DOI:10.1021/jf0505123