دورية أكاديمية
Preparation and characterization of recombinant plant chitinases
| العنوان: | Preparation and characterization of recombinant plant chitinases |
|---|---|
| المؤلفون: | Shobade, Samuel Oluwatoyin |
| المصدر: | Graduate Theses and Dissertations |
| بيانات النشر: | Iowa State University Digital Repository |
| سنة النشر: | 2020 |
| المجموعة: | Digital Repository @ Iowa State University |
| مصطلحات موضوعية: | Basic-EndochitinaseA, Chitinases, EndochitinaseA, Glycoside hydrolases (GHs) 19 |
| الوصف: | Plants are an important form of life. They are required for atmospheric oxygen, chemical energy (Food), medicine, fossilized fuels, and understanding cellular processes critical for survival. Plants have systems of defense composed of physical barriers, chemical messengers, and proteins that detect and respond to pathogen attack. These defenses can be eluded by some specialized fungal pathogens and cause diseases such as anthracnose, rots, and rusts. Plants express chitinases which degrade chitin, a major cell wall component of fungi, and shells of crustaceans, and cuticles of insects. Chitinase and chitinase-like proteins (CLPs) expressed in plants belong to the glycosyl hydrolases family 18 and 19, which exhibit varied functions. Maize chitinases belonging to the GH19 family have been recognized as important in the plant defense against fungal pathogens. They are composed of a small, hevein-like domain attached to a carboxy-terminal chitinase domain. The abundance and the diversity of oligo- and polysaccharides provide a wide range of biological roles attributed either to these carbohydrates or to their relevant enzymes, i.e., the glycoside hydrolases (GHs). The biocatalysis by these families of enzymes is highly attractive for the generation of products used in potential applications, e.g., pharmaceuticals and food industries. It is thus very important to extract and characterize such enzymes, particularly from plant tissues. In this study, two chitinases, EndochitinaseA and Basic-EndochitinaseA of the GH19 family from the roots of Zea mays were cloned, expressed, and characterized. Here, we report an analysis of the activity of the recombinant form of these chitinases under different conditions of salt, temperature, and pH. A modeling analysis of the proteins was also performed. The recombinant maize roots chitinases were purified from both Escherichia coli and HEK293 cells by Ni-NTA column purification. Enzyme activity was evaluated by the DNS method for reducing sugars, using colloidal chitin as substrate. ... |
| نوع الوثيقة: | text |
| وصف الملف: | application/pdf |
| اللغة: | English |
| العلاقة: | https://lib.dr.iastate.edu/etd/18228Test; https://lib.dr.iastate.edu/cgi/viewcontent.cgi?article=9235&context=etdTest |
| الإتاحة: | https://lib.dr.iastate.edu/etd/18228Test https://lib.dr.iastate.edu/cgi/viewcontent.cgi?article=9235&context=etdTest |
| رقم الانضمام: | edsbas.30F9C492 |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |