Recent Trends in Enzymatic Conversion of Cephalosporin C to 7-Aminocephalosporanic Acid (7-ACA)

Parmar, Anupama; Kumar, Harish; Marwaha, Sudeep; Kennedy, John F.

doi:10.1080/0738-859891224194

Cited by 37 publications

(8 citation statements)

References 42 publications

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“…This could be due to the inactivation of catalase in the supernatant due to protein dilution effect or cell mediated degradation. The low stability of DAAO in the solvent permeabilized T. variabilis cells has been reported by various workers and has been attributed either to the low stability of the enzyme or to the leakage of the enzyme from the permeabilized cells (Vicenzi and Hansen, 1993;Parmar et al, 1998). The leakage of enzymes from the permeabilized cells of other yeast has also been documented (Joshi et al, 1989;Flores et al, 1996).…”

Section: Resultsmentioning

confidence: 79%

d-Amino acid oxidase and catalase of detergent permeabilized Rhodotorula gracilis cells and its potential use for the synthesis of α-keto acids

Upadhya

Nagajyothi

Bhat

1999

Process Biochemistry

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Section: Resultsmentioning

confidence: 79%

d-Amino acid oxidase and catalase of detergent permeabilized Rhodotorula gracilis cells and its potential use for the synthesis of α-keto acids

Upadhya

Nagajyothi

Bhat

1999

Process Biochemistry

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“…Both in the presence and in the absence of catalase, this enzymatic reaction has several biotechnological applications, including the production of α-keto acids (1,2) and 7-aminocephalosporanic acid (3), the resolution of a racemic mixture of amino acids (4), as well as the analytic determination of D-amino acid (5). DAAO can be obtained from mammals and microorganisms.…”

Section: Introductionmentioning

confidence: 99%

Characterization and application of d-amino acid oxidase and catalase within permeabilized Pichia pastoris cells in bioconversions

Tan

Song

Zhang

et al. 2007

Appl Biochem Biotechnol

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The high-density fermentation of recombinant Pichia pastoris was carried out in a 1-L fermentor. After 60 h of fermentation, the activities of D-amino acid oxidase (DAAO) and catalase assayed with the permeabilized cells attained 12,532 and 684,800 U/L, respectively. Additionally, the stability of DAAO and catalase within the permeabilized cells was relatively high. The half-life of the two enzymes reached 14.5 and 4.0 d at 30 degrees C, respectively. Furthermore, these permeabilized cells could convert D-phenylalanine into 99% phenylpyruvate within 100 min and could be efficiently reused up to 13 cycles. After being treated with base and heating, these treated permeabilized cells could be reused up to three cycles in a batchwise conversion of cephalosporin C, and about 90% 7-beta-(4-carboxybutanamido)-cephalosporanic acid was ultimately obtained at each cycle.

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“…In the past decades, the production strategy for 7-ACA has shifted from the traditional chemical method (Feehting et al 1968;Morin et al 1969) to an enzymatic method (Parmar et al 1998), due to its environmental and economic benefits. The currently available bioconversion is a two-step enzymatic process employing d-amino acid oxidase and glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase (Alfani et al 1997;Shin et al 1996;Luo et al 2004a).…”

mentioning

confidence: 99%

Characteristic of immobilized cephalosporin C acylase and its application in one-step enzymatic conversion of cephalosporin C to 7-aminocephalosporanic acid

Zhu

Luo

Chang

et al. 2010

World J Microbiol Biotechnol

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Cephalosporin C (CPC) acylase is an enzyme which hydrolyzes CPC to 7-aminocephalosporanic acid (7-ACA) directly, and therefore has great potential in industrial application. In this study, the CPC acylase from a recombinant Escherichia coli was purified to high purity by immobilized metal affinity chromatography, and the CPC acylase was covalently attached to three kinds of epoxy supports, BB-2, ES-V-1 and LX-1000EP. The immobilized CPC acylase with LX-1000EP as the support shows the highest activity (81 U g -1 ) suggesting its potential in industrial 7-ACA production. The activity of immobilized enzyme was found to be optimal at pH between 8.5 and 9.5 and to increase with temperature elevation until 55°C. Immobilized CPC acylase showed good stability at pH between 8.0 and 9.5 and at temperature up to 40°C. To avoid product degradation, the production of 7-ACA utilizing immobilized enzyme was carried out at 25°C, pH 8.5 in a designed reactor. Under optimal reaction conditions, a very high 7-ACA yield of 96.7% was obtained within 60 min. In the results of repeated batch production of 7-ACA, 50% activity of the initial cycle was maintained after being recycled 24 times and the average conversion rate of CPC reached 98%.

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Recent Trends in Enzymatic Conversion of Cephalosporin C to 7-Aminocephalosporanic Acid (7-ACA)

Cited by 37 publications

References 42 publications

d-Amino acid oxidase and catalase of detergent permeabilized Rhodotorula gracilis cells and its potential use for the synthesis of α-keto acids

d-Amino acid oxidase and catalase of detergent permeabilized Rhodotorula gracilis cells and its potential use for the synthesis of α-keto acids

Characterization and application of d-amino acid oxidase and catalase within permeabilized Pichia pastoris cells in bioconversions

Characteristic of immobilized cephalosporin C acylase and its application in one-step enzymatic conversion of cephalosporin C to 7-aminocephalosporanic acid

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