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- Title
向日葵锈菌胞外金属蛋白酶的特性分析.
- Authors
张萌; 景岚; 路妍
- Abstract
To further understand the pathogenic mechanism of sunflower infected by rust, the hydrolytic and biological activity of a novel metalloproteinase (Mep) secreted by Puccinia helianthi were characterized and analized. Protease activity was determined by azocasein method, and its absorbance was measured at 280 nm. Results showed that the protease had hydrolytic activity to azocasein, and the optimum temperature and pH of pure enzyme were 50℃ and 7.0 respectively. It remained stable at pH 5.0-9.0 and below 50℃. The activity of Mep was significantly inhibited by ethylene diamine tetraacetic acid disodium (EDTA), ethylene glycol (2-aminoethyl ether) tetraacetic acid (EGTA) and 1,10-phenanthroline. Ions Ca2+, Zn2+ and Mg2+ could significantly increase the activity of Mep. The results indicated that the enzyme was a metalloproteinase. In addition, qRT-PCR results showed the expression of Mep gene in the process of rust infection of sunflower. The gene expression reached a peak at 48 h after inoculation, and then gradually decreased. It could be proved that Mep was involved in the early infection process of P. helianthi to sunflower.
- Subjects
ETHYLENEDIAMINE; ETHYLENE glycol; GENE expression; PUCCINIA; CALCIUM ions; CASEINS; ETHYLENEDIAMINETETRAACETIC acid; PROTEOLYTIC enzymes; GLYCERYL ethers
- Publication
Chinese Journal of Oil Crop Sciences, 2022, Vol 44, Issue 5, p1081
- ISSN
1007-9084
- Publication type
Article
- DOI
10.19802/j.issn.1007-9084.2021219