Title of article :
Preparation of cross-linked enzyme aggregates of l-aminoacylase via co-aggregation with polyethyleneimine
Author/Authors :
Vaidya، نويسنده , , Bhalchandra K. and Kuwar، نويسنده , , Suyog S. and Golegaonkar، نويسنده , , Sandeep B. and Nene، نويسنده , , Sanjay N. Nene، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2012
Pages :
8
From page :
184
To page :
191
Abstract :
l-Aminoacylase from Aspergillus melleus was co-aggregated with polyethyleneimine and subsequently cross-linked with glutaraldehyde to obtain aminoacylase–polyethyleneimine cross-linked enzyme aggregates (termed as AP-CLEA). Under the optimum conditions, AP-CLEA expressed 74.9% activity recovery and 81.2% aggregation yield. The said method of co-aggregation and cross-linking significantly improved the catalytic stability of l-aminoacylase with respect to temperature and storage. AP-CLEA were employed for enantioselective synthesis of three unnatural amino acids (namely: phenylglycine, homophenylalanine and 2-naphthylalanine) via chiral resolution of their ester-, amide- and N-acetyl derivatives. The enantioselectivity of AP-CLEA was the highest for hydrolysis of amino acid amides; was moderate for hydrolysis of N-acetyl amino acids and was the least for hydrolysis of amino acid esters. Furthermore, AP-CLEA were found to retain more than 92% of the initial activity after five consecutive batches of (RS)-homophenylalanine hydrolysis suggesting an adequate operational stability of the biocatalyst.
Keywords :
Cross-linked enzyme aggregates , l-Aminoacylase , chiral resolution , polyethyleneimine , unnatural amino acids
Journal title :
Journal of Molecular Catalysis B Enzymatic
Serial Year :
2012
Journal title :
Journal of Molecular Catalysis B Enzymatic
Record number :
1715637
Link To Document :
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