Article3 Biotech2017
Recombinant production of Aspergillus Flavus uricase and investigation of its thermal stability in the presence of raffinose and lactose.
Article in 3 Biotech, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- Kinetic and thermostability modulation ofVeterinary research forum : an international quarterly journal · 2026Article
- The role of Gln269Leu mutation on the thermostability and structure of uricase from Aspergillus flavus.Scientific reports · 2025Article
- Recombinant Expression and Functional Assessment of Uricase from a Pertinent Origin of the Enzyme,Iranian journal of biotechnology · 2024Article
- Enhancement of Thermostability ofNanomaterials (Basel, Switzerland) · 2021Article
- Molecular Elucidation of a Urate Oxidase fromInternational journal of molecular sciences · 2021Article
- Enhancement of Pharmaceutical Urate Oxidase Thermostability by Rational Design ofIranian journal of biotechnology · 2020Article
- Structure-Based Immunogenicity Prediction of Uricase from Fungal (Aspergillus flavus), Bacterial (Bacillus subtillis) and Mammalian Sources Using Immunoinformatic Approach.The protein journal · 2020Article
- Efficient purification of a recombinant tag-free thermostable3 Biotech · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aspergillus flavus uricase (Rasburicase) with a molecular mass of 135 kDa is currently used for the treatment of gout and hyperuricemia occurring in tumor lysis syndrome. To characterize the effects of raffinose and lactose osmolytes on the uricase structure, its coding sequence was cloned, expressed in E. coli BL21, and purified by Ni-NTA agarose affinity chromatography. Thermal inactivation studies at 40 °C showed that nearly 15% of UOX activity was preserved, while the presence of raffinose and lactose reduced its activity to 35 and 45% of its original activity, respectively. Investigation of UOX thermal stability at 40 °C in the course of time showed that the enzyme relatively lost almost 60% of its original activity after 40 min, whereas more than 50% of UOX activity is preserved in the presence of lactose. Estimation of thermal inactivation rate constant, k
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