Enzyme-stabilizing activity of seed trypsin inhibitors during desiccation
| Autor: | Keng-Hock Pwee, Ji-Ming Lam, Yii-Leng Chua, Xing-Jun Wang, Wendell Q. Sun |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
chemistry.chemical_classification
Trypsin inhibitor Plant Science General Medicine Biology Trypsin biology.organism_classification Enzyme assay Enzyme chemistry Biochemistry Genetics medicine biology.protein Adenanthera pavonina Bovine serum albumin Protein stabilization Desiccation Agronomy and Crop Science medicine.drug |
| Zdroj: | Plant Science. 142:209-218 |
| ISSN: | 0168-9452 |
| DOI: | 10.1016/s0168-9452(99)00007-2 |
| Popis: | Seeds contain protective proteins which are able to preserve glucose-6-phosphate dehydrogenase (EC 1.1.1.49) activity upon co-dehydration of the enzyme with heat-stable seed protein extracts. Adenanthera pavonina L. (saga) seed extracts, in particular, have high levels of enzyme-preserving activity which not only alleviate the detrimental effects of desiccation in the presence of Tris–HCl and NaCl, but also stabilize enzyme activity in solution. Purification of Adenanthera seed extracts by reversed-phase and weak anion-exchange perfusion chromatography, followed by N-terminal protein sequencing have identified Kunitz-type trypsin inhibitors as the major proteins in one set of enzyme-preserving fractions. A quantitative comparison using various concentrations of purified proteins has demonstrated that soybean Kunitz trypsin inhibitor is as effective (on a mass basis) as bovine serum albumin in preserving enzyme activity, and may be an important protein permitting enzyme dehydration in a seed undergoing desiccation. |
| Databáze: | OpenAIRE |
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