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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

Article 16, Volume 60, Issue 1, April 2020, Page 213-224  XML PDF (1.64 MB)
Document Type: Regular issue (Original Article)
DOI: 10.21608/ejbo.2019.6242.1248
Cited by Scopus (8)
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Authors
Fifi. Reda email 1; Sarah El-Shanawany2
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.
Keywords
Hyaluronidase; Immobilization; Kinetic parameters; Purification
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