Advances in enzymatic transformation of penicillins to 6-aminopenicillanic acid (6-APA)

Parmar, Anupama; Kumar, Harvindra Singh; Marwaha, Sudeep; Kennedy, J. F.

doi:10.1016/s0734-9750(00)00039-2

Cited by 114 publications

(53 citation statements)

References 54 publications

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“…3.5.1.11) is used as a bulk enzyme in the production of 6 aminopenicillanic acid (6-APA) by hydrolysis of penicillin G or V (Shewale and Sudhakaran, 1997;Parmar et al 2000) and more recently in the synthesis of 6-APA and 7 amino-desacetoxycephalosporanic acid (7-ADCA) derived semi-synthetic penicillins and cephalosporins (Illanes and Wilson, 2006;Du et al 2009;Pchelintsev et al 2009). Biocatalyst engineering has been a central issue in penicillin acylase biocatalysis (Kallenberg et al 2005;Chandel et al 2008); substantial improvements in penicillin acylase stabilization have been obtained by directed immobilization to solid supports (Basso et al 2003;Montes et al 2007;Sun et al 2009), aggregation (Rajendhran and Gunasekaran, 2007), site-directed mutagenesis and directed evolution (Rajendhran and Gunasekaran, 2004;Serra et al 2009), and functional screening (Gabor et al 2005).…”

mentioning

confidence: 99%

Diffusional restrictions in glyoxyl-agarose immobilized penicillin G acylase of different particle size and protein loading

Illanes¹,

González²,

Gómez³

et al. 2010

Electro Journal of Biotech

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factors at different bulk substrate concentrations were determined for all biocatalysts, values ranging from 0.78 for small particle size at 25 mM penicillin G to 0.15 for large particle size at 2 mM penicillin G. Enzyme protein loading had a strong impact on the effectiveness factors of immobilized penicillin G acylase, being it more pronounced in the case of large particle size biocatalysts. At conditions in which 6-aminopenicillanic acid is industrially produced, all biocatalysts tested were mass-transfer limited, being this information valuable for reactor design and performance evaluation.

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confidence: 99%

Diffusional restrictions in glyoxyl-agarose immobilized penicillin G acylase of different particle size and protein loading

Illanes¹,

González²,

Gómez³

et al. 2010

Electro Journal of Biotech

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“…They are the most widely used β-lactam antibiotics, with a share of about 19 % of the estimated world-wide antibiotic market. (43) In particular, they are effective against the microorganisms responsible for several diseases such as tetanus, diphtheria, syphilis, gonorrhoea and skin boils. Penicillin acylase catalyses the hydrolysis of penicillin G (PG) to phenyl acetic acid (PAA) and 6-aminopenicillanic acid (6-APP) (Figure 10), (44) which is the building block for production of semi-synthetic β-lactam antibiotics, (45) as shown in Table 2.…”

Section: A) Penicillin Acylasementioning

confidence: 99%

Low-Cost Foods and Drugs Using Immobilized Enzymes on Biopolymers

Elnashar¹

2010

Biopolymers

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“…Enzyme immobilization is proven to be one of the key steps in making the enzymatic processes economically practicable (Cao and Schmid 2005;Zhou 2009). According to the study of Parmar et al (2000), it is also found that the immobilized enzyme catalyst with the improved activity and stability can reduce the production cost. Cross-linking enzyme aggregate (CLEA) is described as the latest enzyme immobilization technology (Barbosa et al 2014;Brady and Jordaan 2009;Sheldon et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Mahmod

Yusof

Jami

et al. 2016

Bioresour. Bioprocess.

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Background: Cross-linked enzyme aggregate (CLEA) is considered as an effective technique in the production of immobilized biocatalysts for its industrially attractive advantages. Simplicity, stability, low cost, time saving and reusability are proved to be some of CLEA's main advantages. Results:In this study, an active, stable and recyclable CLEA-protease from the viscera of channel catfish Ictalurus punctatus has been prepared. Optimization of the preparation parameters is carried out with the help of Response Surface Methodology. This methodology helped in studying the interaction between the most contributing factors such as cross-linker, precipitant and the additive concentrations. The optimum specific activity for CLEA-protease of 4.512 U/mg protein has shown a high stability against the denaturation forces such as temperature and pH as compared to free protease. It is further found from the study that the highest activity was achieved at the pH of 6.8 and at the temperature of 45 °C. After six cycles, CLEA-protease maintained 28 % of its original activity. Additionally, Michaelis-Menten models were used to determine the kinetic parameters i.e. K m and V max that helped in showing a significant difference after immobilization as compared to free protease. Conclusion:This work found that this novel CLEA-protease can be used as a very active biocatalyst in industrial applications.

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Advances in enzymatic transformation of penicillins to 6-aminopenicillanic acid (6-APA)

Cited by 114 publications

References 54 publications

Diffusional restrictions in glyoxyl-agarose immobilized penicillin G acylase of different particle size and protein loading

Diffusional restrictions in glyoxyl-agarose immobilized penicillin G acylase of different particle size and protein loading

Low-Cost Foods and Drugs Using Immobilized Enzymes on Biopolymers

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

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