Literature DB >> 12675578

Highly multilayered urease decomposes highly concentrated urea.

Satoshi Kobayashi1, Shinji Yonezu, Hidetaka Kawakita, Kyoichi Saito, Kazuyuki Sugita, Masao Tamada, Takanobu Sugo, William Lee.   

Abstract

Urease was immobilized at a density of 1.2 g of urease per gram of a matrix via ion-exchange binding of urease to an anion-exchange polymer chain grafted onto a pore surface of a porous hollow-fiber membrane and subsequent cross-linking of urease with transglutaminase. Urea was hydrolyzed during the permeation of a urea solution, the concentration of which ranged from 2 to 8 M, through the pores of the resultant membrane with a thickness of approximately 1 mm. Quantitative hydrolysis of 4 M urea was achieved at a permeation rate lower than 1 mL/h, i.e., a residence time longer than 5.1 min, at ambient temperature. This performance is ascribed to convective transport of urea through the pores rimmed by the urease-immobilized polymer chains at a high density. Urease was denatured in the presence of urea at concentrations higher than 6 M while hydrolyzing urea.

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Year:  2003        PMID: 12675578     DOI: 10.1021/bp020072p

Source DB:  PubMed          Journal:  Biotechnol Prog        ISSN: 1520-6033


  1 in total

1.  Substrate catalysis enhances single-enzyme diffusion.

Authors:  Hari S Muddana; Samudra Sengupta; Thomas E Mallouk; Ayusman Sen; Peter J Butler
Journal:  J Am Chem Soc       Date:  2010-02-24       Impact factor: 15.419

  1 in total

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