| Autor: |
Mahmoud H. Hendy, Amr H. Hashem, Waleed B. Suleiman, Mahmoud H. Sultan, Mohamed Abdelraof |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
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| Zdroj: |
Microbial Cell Factories, Vol 22, Iss 1, Pp 1-11 (2023) |
| Druh dokumentu: |
article |
| ISSN: |
1475-2859 |
| DOI: |
10.1186/s12934-023-02019-z |
| Popis: |
Abstract Purification of L-methionine γ-lyase (MGL) from A. fumigatus was sequentially conducted using heat treatment and gel filtration, resulting in 3.04 of purification fold and 73.9% of enzymatic recovery. The molecular mass of the purified MGL was approximately apparent at 46 KDa based on SDS-PAGE analysis. The enzymatic biochemical properties showed a maximum activity at pH 7 and exhibited plausible stability within pH range 5.0–7.5; meanwhile the highest catalytic activity of MGL was observed at 30–40 °C and the enzymatic stability was noted up to 40 °C. The enzyme molecule was significantly inhibited in the presence of Cu2+, Cd2+, Li2+, Mn2+, Hg2+, sodium azide, iodoacetate, and mercaptoethanol. Moreover, MGL displayed a maximum activity toward the following substrates, L-methionine |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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