Repository of Research and Investigative Information

Repository of Research and Investigative Information

Ilam University of Medical Sciences

Overexpression and Enzymatic Assessment of Antigenic Fragments of Hyaluronidase Recombinant Protein From Streptococcus pyogenes

Fri May 20 01:46:52 2022

(2015) Overexpression and Enzymatic Assessment of Antigenic Fragments of Hyaluronidase Recombinant Protein From Streptococcus pyogenes. Jundishapur Journal of Microbiology. p. 6. ISSN 2008-3645

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Abstract

Background: Hyaluronidase catalyzes the hydrolysis of hyaluronan polymers to N-acetyl-D-glucosamine and D-glucuronic acid. This enzyme is a dimer of identical subunits. Hyaluronidase has different pharmaceutical and medical applications. Previously, we produced a recombinant hyaluronidase antigenic fragment of Streptococcus pyogenes. Objectives: This study aimed to improve the protein production and purity of hyaluronidase recombinant protein from S. pyogenes. In addition, the enzymatic activity of this protein was investigated. Materials and Methods: The expression of hyaluronidase antigenic fragments was optimized using IPTG concentration, time of induction, temperature, culture, and absorbance of 0.6-0.8-1 at 600 nm. Afterwards, the expressed proteins were purified and the enzymatic activity was assessed by turbid metric method. Results: Data indicated that maximum protein is produced in OD = 0.8, 0.5 mM Isopropyl beta-D-1-thiogalactopyranoside (IPTG), 37 degrees C, NB 1.5x, without glucose, incubated for overnight. The enzymatic activity of the recombinant protein was similar to the commercial form of hyaluronidase. Conclusions: The results showed that an antigenic fragment of the recombinant hyaluronidase protein from S. pyogenes has a considerable enzymatic activity. It can be suggested to use it for medical purposes. In addition, applications of bioinformatics software would facilitate the production of a smaller protein with same antigenic properties and enzymatic activity.

Item Type: Article
Creators:
CreatorsEmail
Abbasian, S. S.UNSPECIFIED
Rad, E. G.UNSPECIFIED
Akbari, N.UNSPECIFIED
Zolfaghari, M. R.UNSPECIFIED
Pakzad, I.UNSPECIFIED
Abtahi, H.UNSPECIFIED
Keywords: Hyaluronidase Optimization of Expression Enzymatic Activity escherichia-coli assay venom degradation sensitivity inhibitors virulence cancer Microbiology
Divisions:
Page Range: p. 6
Journal or Publication Title: Jundishapur Journal of Microbiology
Journal Index: ISI
Volume: 8
Number: 1
Identification Number: https://doi.org/10.5812/jjm.13653
ISSN: 2008-3645
Depositing User: مهندس مهدی شریفی
URI: http://eprints.medilam.ac.ir/id/eprint/606

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