Reda, F., El-Shanawany, S. (2020). Characterization and Immobilization of a Novel Hyaluronidase Produced by Streptomyces roseofulvus . Egyptian Journal of Botany, 60(1), 213-224. doi: 10.21608/ejbo.2019.6242.1248
Fifi. Reda; Sarah El-Shanawany. "Characterization and Immobilization of a Novel Hyaluronidase Produced by Streptomyces roseofulvus ". Egyptian Journal of Botany, 60, 1, 2020, 213-224. doi: 10.21608/ejbo.2019.6242.1248
Reda, F., El-Shanawany, S. (2020). 'Characterization and Immobilization of a Novel Hyaluronidase Produced by Streptomyces roseofulvus ', Egyptian Journal of Botany, 60(1), pp. 213-224. doi: 10.21608/ejbo.2019.6242.1248
Reda, F., El-Shanawany, S. Characterization and Immobilization of a Novel Hyaluronidase Produced by Streptomyces roseofulvus . Egyptian Journal of Botany, 2020; 60(1): 213-224. doi: 10.21608/ejbo.2019.6242.1248
Characterization and Immobilization of a Novel Hyaluronidase Produced by Streptomyces roseofulvus
1Department of Botany and Microbiology, Faculty of Science, Zagazig University, 44519, Zagazig, Egypt
2Department of Botany and Microbiology, Faculty of Science, Zagazig University, 44519, Zagazig, Egypt
Abstract
M AXIMUM hyaluronidase production by Streptomyces roseofulvus S10 (LC314796) was attained when it was cultured in submerged fermentation process under favorable conditions, pH 5 at 40ºC for 6 days. Hyaluronidase was purified to its homogeneity by 9.2 fold with molecular weight of 97kDa under denaturing SDS- PAGE. Mg+2 exerted highly stimulatory effect on S. roseofulvus S10 hyaluronidase activity and was significantly reduced in presence of Mn+2, Zn+2, and EDTA. Optimum reaction was attained at pH 9 and the pH stability of enzyme ranged between 9-10 at 35°C. To protect the intrinsic activity and half-time of hyaluronidase, several carriers and immobilization of hyaluronidase were investigated. The immobilized enzyme had higher thermal stability than free one with Tm values; 46.1°C and 24.7°C, respectively. Maximum affinity of free and immobilized hyaluronidase was for hyaluronic acid followed by bovine albumin. Free enzyme had a high catalytic affinity of hyaluronic acid compared with immobilized enzyme. Our results demonstrated that S. roseofulvus S10 hyaluronidase was highly stable to pH and high temperature. These properties of long-term stability facilitate its wide range of applications.
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