Antimicrobial activity studies on a trypsin-chymotrypsin protease inhibitor obtained from potato |
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Authors: | Kim Jin-Young Park Seong-Cheol Kim Mi-Hyun Lim Hak-Tae Park Yoonkyung Hahm Kyung-Soo |
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Institution: | Research Center for Proteineous Materials (RCPM), Chosun University, 375 Seosuk-Dong, Dong-Ku, Kwangju 501-759, Republic of Korea. |
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Abstract: | A 5.6 kDa trypsin-chymotrypsin protease inhibitor was isolated from the tubers of the potato (Solanum tuberosum L cv. Gogu) by extraction of the water-soluble fraction, dialysis, ultrafiltration, and C18 reversed-phase high performance liquid chromatography. This inhibitor, which we named potamin-1 (PT-1), was thermostable and possessed antimicrobial activity but lacked hemolytic activity. PT-1 strongly inhibited pathogenic microbial strains, including Candida albicans, Rhizoctonia solani, and Clavibacter michiganense subsp. michiganinse. Automated Edman degradation showed that the N-terminal sequence of PT-1 was NH2-DICTCCAGTKGCNTTSANGAFICEGQSDPKKPKACPLNCDPHIAYA-. The sequence had 62% homology with a serine protease inhibitor belonging to the Kunitz family, and the peptide inhibited chymotrypsin, trypsin, and papain. This protease inhibitor, PT-1, was composed of polypeptide chains joined by disulfide bridge(s). Reduced PT-1 almost completely lost its activity against fungi and proteases indicating that disulfide bridge is essential for its protease inhibitory and antifungal activity. These results suggest that PT-1 is an excellent candidate as a lead compound for the development of novel oral or other anti-infective agents. |
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Keywords: | Antimicrobial activity trypsin-chymotrypsin protease inhibitor Kunitz family Anti-infective agents |
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