A simple purification procedure of D-amino-acid oxidase from Candida guilliermondii

Gevorgyan, G. K.; Davtyan, M. A.; Hambardzumyan, A. A.

doi:10.1134/s0026261712040078

Microbiology

2012

DOI: 10.1134/s0026261712040078

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A simple purification procedure of D-amino-acid oxidase from Candida guilliermondii

G. K. Gevorgyan

M. A. Davtyan

A. A. Hambardzumyan

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Cited by 2 publications

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“…PEGylated lysozyme, human transferrin) or chemically similar variants (e.g. deaminated protein variants) or as an intermediate purification step of d-amino acid oxidase from Candida guilliermondii [23][24][25][26].…”

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confidence: 99%

Systematic purification of salt‐intolerant proteins by ion‐exchange chromatography: The example of human α‐galactosidase A

Baumann

Osberghaus

Hubbuch

2015

Engineering in Life Sciences

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Chromatography is an essential tool for purifying biopharmaceutical products. Many processes are still developed based on traditional routines and empirical procedures. Product losses are mostly due to insufficient optimization of purification setups and product sensitivity to process conditions. In order to eliminate these shortcomings, a systematic strategy for the setup of ion‐exchange chromatography is presented, which considers both product stability as well as operational conditions. The stages—a hybrid approach combining high‐throughput screening and analytical small‐scale chromatography—are as follows: (1) pH stability (short‐term); (2) pH stability (long‐term), followed by a screening of additives to enhance protein stability, if required; (3) analytical pH gradient chromatography for evaluation of the operational pH window; and (4) salt stability (long‐term) in the operational pH window determined. The efficiency and straightforwardness of the strategy were shown in a case study on capturing the human α‐galactosidase A enzyme. Following the above procedure, the enzyme was found to be salt‐unstable; a purification factor of 13.2, a concentration factor of 4, and an overall yield of 84.3% were achieved. The applied strategy allowed for a quick establishment of a dedicated capture step at low salt concentrations under stable conditions by well‐chosen prior screening experiments.

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mentioning

confidence: 99%

Systematic purification of salt‐intolerant proteins by ion‐exchange chromatography: The example of human α‐galactosidase A

Baumann

Osberghaus

Hubbuch

2015

Engineering in Life Sciences

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d-Amino acid oxidase and presence of d-proline in Xenopus laevis

Soma

Furuya

Kaneko

et al. 2013

Comparative Biochemistry and Physiology Part B: Biochemistry an

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A simple purification procedure of D-amino-acid oxidase from Candida guilliermondii

Cited by 2 publications

References 23 publications

Systematic purification of salt‐intolerant proteins by ion‐exchange chromatography: The example of human α‐galactosidase A

Systematic purification of salt‐intolerant proteins by ion‐exchange chromatography: The example of human α‐galactosidase A

d-Amino acid oxidase and presence of d-proline in Xenopus laevis

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