A. Márquez, Nayeli Soria- Calderón, M. G. Villa-Rivera, Everardo López- Romero, Nancy Calderón- Cortés
{"title":"嗜木食昆虫变形蛇(鞘翅目:天牛科)聚半乳糖醛酸酶的纯化及特性研究","authors":"A. Márquez, Nayeli Soria- Calderón, M. G. Villa-Rivera, Everardo López- Romero, Nancy Calderón- Cortés","doi":"10.7324/jabb.2022.100402","DOIUrl":null,"url":null,"abstract":"In this work we purified a polygalacturonase enzyme from the midgut of larvae of the xylophagous insect Oncideres albomarginata chamela . The polygalacturonase showed high enzymatic activity (390.7 U/mg) in the crude extract and was purified to apparent homogeneity by means of cation exchange chromatography, hydrophobic interaction chromatography, and gel filtration. The molecular mass of the polygalacturonase was estimated to be 37 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme had an optimum pH of 6.0 and an optimum temperature of 50°C. According to the kinetic studies on polygalacturonic acid, the polygalacturonase showed a Km of 3.18 mg/ml and Vmax of 716.15 U/mg. The enzymatic properties of the purified enzyme correspond to those reported for highly active commercially produced enzymes, highlighting the potential of this insect enzyme to be used in industrial applications.","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"64 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Purification and characterization of a polygalacturonase from the xylophagous insect Oncideres albomarginata chamela (Coleoptera: Cerambycidae)\",\"authors\":\"A. Márquez, Nayeli Soria- Calderón, M. G. Villa-Rivera, Everardo López- Romero, Nancy Calderón- Cortés\",\"doi\":\"10.7324/jabb.2022.100402\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"In this work we purified a polygalacturonase enzyme from the midgut of larvae of the xylophagous insect Oncideres albomarginata chamela . The polygalacturonase showed high enzymatic activity (390.7 U/mg) in the crude extract and was purified to apparent homogeneity by means of cation exchange chromatography, hydrophobic interaction chromatography, and gel filtration. The molecular mass of the polygalacturonase was estimated to be 37 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme had an optimum pH of 6.0 and an optimum temperature of 50°C. According to the kinetic studies on polygalacturonic acid, the polygalacturonase showed a Km of 3.18 mg/ml and Vmax of 716.15 U/mg. The enzymatic properties of the purified enzyme correspond to those reported for highly active commercially produced enzymes, highlighting the potential of this insect enzyme to be used in industrial applications.\",\"PeriodicalId\":423079,\"journal\":{\"name\":\"Journal of Applied Biology & Biotechnology\",\"volume\":\"64 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2022-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Applied Biology & Biotechnology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.7324/jabb.2022.100402\",\"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 Applied Biology & Biotechnology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.7324/jabb.2022.100402","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification and characterization of a polygalacturonase from the xylophagous insect Oncideres albomarginata chamela (Coleoptera: Cerambycidae)
In this work we purified a polygalacturonase enzyme from the midgut of larvae of the xylophagous insect Oncideres albomarginata chamela . The polygalacturonase showed high enzymatic activity (390.7 U/mg) in the crude extract and was purified to apparent homogeneity by means of cation exchange chromatography, hydrophobic interaction chromatography, and gel filtration. The molecular mass of the polygalacturonase was estimated to be 37 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme had an optimum pH of 6.0 and an optimum temperature of 50°C. According to the kinetic studies on polygalacturonic acid, the polygalacturonase showed a Km of 3.18 mg/ml and Vmax of 716.15 U/mg. The enzymatic properties of the purified enzyme correspond to those reported for highly active commercially produced enzymes, highlighting the potential of this insect enzyme to be used in industrial applications.