Recombinant Expression and Functional Assessment of Uricase from a Pertinent Origin of the Enzyme, Streptomyces sp. Strain 17-1

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Nasir Shirazi Mohaddeseh; Sarikhan Sajjad; Ghafouri Hossein; Amirmojahedi Hamideh; Moshtaghi Nikoo Mahdi; Shahzadeh Fazeli Seyed Abolhassan; Amoozgar Mohammad Ali

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Journal Paper

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Journal: IRANIAN JOURNAL OF BIOTECHNOLOGY Year:2024 | Volume:22 | Issue:1 Page(s): 65-75

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Title

Recombinant Expression and Functional Assessment of Uricase from a Pertinent Origin of the Enzyme, Streptomyces sp. Strain 17-1

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Keywords

Actinobacteria

pET28a+

Streptomyces

Uricase

Abstract

Background: Uricase or urate oxidase, as a therapeutic enzyme, is extensively applied to oxidize accumulated uric acidin the body to soluble form to treat related illnesses.Objectives: This study was conducted with the aim of searching for potential sources of uricase-producing Streptomycesfrom Eshtehard salt desert in Alborz province, Iran and heterologous expression, purification and functional assay of theenzyme.Materials and Methods: Main screening was conducted by cultivation of the strains on a medium enriched with 0.3 percent (w/v) uric acid. The uricase gene from the most potent strain was then recombinantly expressed in E. coli BL21 (DL3)Results:Out of the tested strains, only seven showed uricase activity. The highest level of native uricase activity (11.5735U.mL-1) belonged to strain 17-1, which had the closest similarity to Streptomyces nigra. A recombinant uricase witha molecular mass of approximately 38 kDa was produced. The purified uricase exhibited a specific activity of about28.29±0.59 U.mg-1, which is among the highest level of uricase activity reported by other studiesConclusions: This enzyme is a promising candidate for further applicable investigations and large-scale production interms of its large volume of soluble expression and selective competitive activity.

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