Purification and Immobilization of Aginase from Fenugreek Plants | ||||
| Egyptian Journal of Chemistry | ||||
| Volume 66, Issue 1, January 2023, Page 447-452 PDF (592.98 K) | ||||
| Document Type: Review Articles | ||||
| DOI: 10.21608/ejchem.2022.124718.5553 | ||||
 View on SCiNiTO | ||||
| Authors | ||||
Alyaa Ibrahim Mohamed1; Hamed M. El-Shora1; Neven Ahmad Salah  2; Magdy M. Yousef 1
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| 1Chemistry Department Faculty of Science Mansoura University Mansoura Egypt | ||||
| 2Biochemistry Division-Chemistry Depatment- Faculty of Science-Mansoura University- Egypt | ||||
| Abstract | ||||
| Abstract: Introduction: Enzymes are recorded in all living organisms where they speed up and regulate the chemical reactions that crucial for the life of organisms. L-Arginase (L-arginine urea hydrolase, or amidinohydrolase, EC 3.5.3.1) is hydrolytic enzyme. It is a divalent cation-dependent and plays an essential role in nitrogen metabolism through converting L-arginine to L-ornithine plus urea. Aim of the work: This work aimed to isolate, purify and comparing the characteristics of the free and immobilized L-arginase from Fenugreek. Material and methods: L-arginase was purified from fenugreek plants. L-arginase was purified successfully to homogeneity from fenugreek by 80 % ammonium sulphate, DEAE-cellulose and Sephadex G200. L-arginase was immobilized on calcium alginate and chitosan. Reuse of immobilized L-arginase was tested through 7 cycles. Results: The results in the present investigation showed that the optimal pH for the free L-arginase was 8.5 whereas the immobilized enzyme expressed optimal pH at 9.0. On studying the effect of temperature on the free and immobilized enzyme showed that the optimal temperature was 40°C for the free enzyme and shifted to 50ºC for the immobilized form on both Ca alginate and chitosan. Conclusion: The presence of L-arginase in fenugreek suggests that this plant may be a potential plant source for developing the industrial biosynthetic production of L-ornithine. | ||||
| Keywords | ||||
| L-arginase; Purification; Characterization; Active site groups; Immobilization; Applications | ||||
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