0000000001072687

AUTHOR

L. Volpe

showing 1 related works from this author

Optimization of a Biotechnological Process for Production and Purification of Two Recombinant Proteins: Col G and Col H

2017

Different strategies can be used for increasing production of heterologous recombinant proteins in Escherichia coli. Protein size is often critical for obtaining the best quantity/quality ratio of recombinant protein expression. This study focuses on two recombinant proteins; Class I and class II Collagenases, namely Col G and Col H. Their size is about 150 kDa each. We have developed a method to obtain high levels of cell growth and intracellular expression of each Collagenases in recombinant E. coli BL21(DE3). Batch and Fed-batch fermentation procedures have been performed. Results show that Fed-batch technique was most effective in obtaining the highest cell density for each recombinant …

collagenasecollagenases; E.coli; fermentation; downstream purification;downstream purificationSettore BIO/10 - BiochimicaE.colifermentation
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