Purification and characterization of a caseinolytic enzyme from Bacillus subtilis.
Elkenawi, E., Elsayed, A., El-Senduny, F., Youssef, M. (2022). Purification and characterization of a caseinolytic enzyme from Bacillus subtilis.. EKB Journal Management System, 55(1), 27-31. doi: 10.21608/mjcc.2022.412087
Ebtesam G. Elkenawi; A Elsayed; Fardous F. El-Senduny; Magdy M. Youssef. "Purification and characterization of a caseinolytic enzyme from Bacillus subtilis.". EKB Journal Management System, 55, 1, 2022, 27-31. doi: 10.21608/mjcc.2022.412087
Elkenawi, E., Elsayed, A., El-Senduny, F., Youssef, M. (2022). 'Purification and characterization of a caseinolytic enzyme from Bacillus subtilis.', EKB Journal Management System, 55(1), pp. 27-31. doi: 10.21608/mjcc.2022.412087
Elkenawi, E., Elsayed, A., El-Senduny, F., Youssef, M. Purification and characterization of a caseinolytic enzyme from Bacillus subtilis.. EKB Journal Management System, 2022; 55(1): 27-31. doi: 10.21608/mjcc.2022.412087

Purification and characterization of a caseinolytic enzyme from Bacillus subtilis.

Mansoura Journal of Chemistry
Volume 55, Issue 1, February 2022, Page 27-31  XML PDF (600.59 K)
Document Type: Original Article
DOI: 10.21608/mjcc.2022.412087
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Authors
Ebtesam G. Elkenawi* 1; A Elsayed2; Fardous F. El-Senduny3; Magdy M. Youssef4
1Chemistry Department,Faculty of Science, Mansoura University, Mansoura
2Botany Department, Faculty of Science, Mansoura University, Mansoura
3Chemistry Department, Faculty of Science, Mansoura University, Mansoura
4Chemistry Department, Faculty of Science, Mansoura University, Mansoura
Abstract
Nattokinase (EC 3.4.21.62) is a serine protease and profibrinolytic enzyme with a strong fibrin-degrading activity, and many host strains can produce it. By its comparison with other fibrinolytic enzymes such as (streprokinase, urokinase and t-PA), nattokinase showed many advantages of having long life-time, no side effects, costless and it owns the ability to be a drug candidate for treatment of heart diseases and used as an effective food additive. Bacillus subtilis natto discovered in natto, a typical Japanese fermented soybean food. After the purification of Nattokinase from the supernatant of B. subtilis culture media, it showed a strong fibrinolytic activity. The enzyme was refined to a 4.4-fold purity level, with 61.8 percent of activity recovered. SDS-PAGE showed that nattokinase is homogenous and identified it as a monomer of 29000 Da in its original state. The optimum temperature and pH were 65°c and 9.0 respectively. Purified nattokinase is thermally stable at temperatures ranging from 35 to 55 °C and alkaline stable at pH 7.0 to 10.0. Skim milk agar showed clear zone of crude enzyme. Mg2+ increased the activity of nattokinase, but Zn2+ and Fe3+ decreased the activity. Triton x-100 as detergent significantly increased activity of nattokinase on the contrast to SDS inhibit nattokinase activity.
Keywords
Nattokinase; Bacillus subtilis; Skim milk; TritonX-100
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