{"title":"部门芽孢杆菌FERM-P8973普鲁兰酶的纯化及性质研究","authors":"Y. Sakano, T. Tonozuka, D. Fujimoto","doi":"10.5458/JAG1972.39.7","DOIUrl":null,"url":null,"abstract":"A pullulanase ([EC 3.2.1.41] pullulan 6-glucanohydrolase) from Bacillus sectorramus FERMP8973 (Amano Pharmaceutical Co . Ltd., ) was purified using Mono Q anion-exchange chromatography. Purified enzyme showed a single band on PAGE and SDS-PAGE, and a single peak on HPLC on a TSK-gel G3000SW . The molecular weight (95 kD), optimum pH (5-5.5), optimum temperature (55°C), pH stability and thermal stability were similar to the results of Mori et al. (Denpun Kagaku, 38, 9-16, 1991), but the isoelectric point (5 .3) was different from their result (4.7). Its amino acid composition was similar to those of other amylases. Its Nterminal amino acid sequence was YSNSTGVIVHTHRDSNYTN-, and thus did not resemble those of Klebsiella pneumoniae W70 pullulanase having a collagen-like sequence.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"39 1","pages":"7-9"},"PeriodicalIF":0.0000,"publicationDate":"1992-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Purification and Properties of Bacillus sectorramus FERM-P8973 Pullulanase\",\"authors\":\"Y. Sakano, T. Tonozuka, D. Fujimoto\",\"doi\":\"10.5458/JAG1972.39.7\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"A pullulanase ([EC 3.2.1.41] pullulan 6-glucanohydrolase) from Bacillus sectorramus FERMP8973 (Amano Pharmaceutical Co . Ltd., ) was purified using Mono Q anion-exchange chromatography. Purified enzyme showed a single band on PAGE and SDS-PAGE, and a single peak on HPLC on a TSK-gel G3000SW . The molecular weight (95 kD), optimum pH (5-5.5), optimum temperature (55°C), pH stability and thermal stability were similar to the results of Mori et al. (Denpun Kagaku, 38, 9-16, 1991), but the isoelectric point (5 .3) was different from their result (4.7). Its amino acid composition was similar to those of other amylases. Its Nterminal amino acid sequence was YSNSTGVIVHTHRDSNYTN-, and thus did not resemble those of Klebsiella pneumoniae W70 pullulanase having a collagen-like sequence.\",\"PeriodicalId\":17372,\"journal\":{\"name\":\"Journal of the Japanese Society of Starch Science\",\"volume\":\"39 1\",\"pages\":\"7-9\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1992-03-31\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of the Japanese Society of Starch Science\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.5458/JAG1972.39.7\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the Japanese Society of Starch Science","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.5458/JAG1972.39.7","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification and Properties of Bacillus sectorramus FERM-P8973 Pullulanase
A pullulanase ([EC 3.2.1.41] pullulan 6-glucanohydrolase) from Bacillus sectorramus FERMP8973 (Amano Pharmaceutical Co . Ltd., ) was purified using Mono Q anion-exchange chromatography. Purified enzyme showed a single band on PAGE and SDS-PAGE, and a single peak on HPLC on a TSK-gel G3000SW . The molecular weight (95 kD), optimum pH (5-5.5), optimum temperature (55°C), pH stability and thermal stability were similar to the results of Mori et al. (Denpun Kagaku, 38, 9-16, 1991), but the isoelectric point (5 .3) was different from their result (4.7). Its amino acid composition was similar to those of other amylases. Its Nterminal amino acid sequence was YSNSTGVIVHTHRDSNYTN-, and thus did not resemble those of Klebsiella pneumoniae W70 pullulanase having a collagen-like sequence.
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