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Purification and characterization of a heat-stable serine protease inhibitor from the tubers of new potato variety "Golden Valley" |
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| Authors: | Kim Mi-Hyun Park Seong-Cheol Kim Jin-Young Lee Sun Young Lim Hak-Tae Cheong Hyeonsook Hahm Kyung-Soo Park Yoonkyung |
| Institution: | a Research Center for Proteineous Materials (RCPM), Chosun University, Kwangju 501-759, Republic of Korea b Department of Medicine, Chosun University, Kwangju 501-759, Republic of Korea c Department of Biotechnology, Chosun University, Kwangju 501-759, Republic of Korea d Division of Biotechnology, Kangwon National University, 192-1, Hyoja2-Dong, Chunchon, Kangwon-Do 200-701, Republic of Korea e Division of Applied Life Science, Gyeongsang National University, Chinju 660-701, Republic of Korea |
| Abstract: | Potide-G, a small (5578.9 Da) antimicrobial peptide, was isolated from potato tubers (Solanum tuberosum L. cv. Golden Valley) through extraction of the water-soluble fraction, dialysis, ultrafiltration and DEAE-cellulose and C18 reverse-phase high performance liquid chromatography. This antimicrobial peptide was heat-stable and almost completely suppressed the proteolytic activity of trypsin, chymotrypsin and papain, with no hemolytic activity. In addition, potide-G potently inhibited growth of a variety of bacterial (Staphylococcus aureus, Listeria monocytogenes, Escherichia coli, and Clavibacter michiganense subsp. michiganinse) and fungal (Candida albicans and Rhizoctonia solani) strains. Matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry revealed that the N-terminal sequence (residues from 1 to 11) of the protein is identical to that of potato proteinase inhibitor, a member of the Kunitz superfamily. And like other members of this class of protease inhibitor, potide-G may have a number of beneficial and therapeutic uses. |
| Keywords: | Antimicrobial peptide Proteinase inhibitor Inhibition activity Perianal dermatitis |
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