Cross-Linked Enzyme Aggregates of Naringinase: Novel Biocatalysts for Naringin Hydrolysis

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Cross-Linked Enzyme Aggregates of Naringinase: Novel Biocatalysts for Naringin Hydrolysis

Cross-linked enzyme aggregates (CLEAs) have emerged as interesting biocatalyst design for immobilization. These new generation enzyme biocatalysts, CLEAs, in addition to exhibiting good mechanical stability, can be highly active, since they do not include large amounts of foreign particulate nonenzymatic material and may have increased stability. Naringinase (NGase) is an enzyme complex with hi...

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Cross-linked enzyme aggregates (CLEAs): stable and recyclable biocatalysts.

The key to obtaining an optimum performance of an enzyme is often a question of devising an effective method for its immobilization. In the present review, we describe a novel, versatile and effective methodology for enzyme immobilization as CLEAs (cross-linked enzyme aggregates). The method is exquisitely simple (involving precipitation of the enzyme from aqueous buffer followed by cross-linki...

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Use of Cross-Linked Enzyme Aggregates (CLEAs) for performing biotransformations

The methodology for the preparation of cross-linked enzyme aggregates (CLEAs) and their application as highly effective, recyclable biocatalysts in a wide variety of transformations is reviewed. The method constitutes a combination of enzyme purification and immobilization into a single operation and allows for the use of relatively crude enzyme preparations. The resulting CLEAs have excellent ...

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Cross-linked Enzyme Aggregates of Catalase from Bovine Liver

Stabilization of multimeric enzymes is one of the major challenges in biocatalysis, because dissociation of subunits can inactivate the enzyme. Catalase (CAT; EC 1.11.16) is a homotetramer containing Fe-protoporphyrin IX in its active site. CAT breaks down hydrogen peroxide into water and molecular oxygen. In this study, crosslinked enzyme aggregates of bovine liver CAT (CAT-CLEAs) were prepare...

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Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase

Penicillin G acylase from E. coli TA1 was immobilized by Cross-Linked Enzyme Aggregates (CLEA), a new method for immobilization. This biocatalyst and commercial immobilized penicillin G acylase (PGA-450) were used to study the effect of pH, temperature and substrate concentration on the synthesis of ampicillin from phenyl glycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA). Compare...

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ژورنال

عنوان ژورنال: Enzyme Research

سال: 2011

ISSN: 2090-0414

DOI: 10.4061/2011/851272