High level production of a cellulase-free xylanase in glucose-limited fed batch cultures of a thermophilic Bacillus strain

1997 ◽  
Vol 58 (2) ◽  
pp. 71-78 ◽  
Author(s):  
E Samain ◽  
Ph Debeire ◽  
J.P Touzel
Keyword(s):  
Fed Batch ◽  
Batch Cultures ◽  
Thermophilic Bacillus ◽  
Bacillus Strain ◽  
High Level ◽  
Level Production

High-level production of arachidonic acid by fed-batch culture of Mortierella alpina using NH4OH as a nitrogen source and pH control

2005 ◽  
Vol 27 (10) ◽  
pp. 731-735 ◽  
Author(s):  
Byung-Hae Hwang ◽  
Jin-Wook Kim ◽  
Chang-Yeol Park ◽  
Chang-Seo Park ◽  
Yong-Sung Kim ◽  
...  
Keyword(s):  
Arachidonic Acid ◽  
Nitrogen Source ◽  
Batch Culture ◽  
Ph Control ◽  
Mortierella Alpina ◽  
Fed Batch ◽  
Fed Batch Culture ◽  
High Level ◽  
Level Production

scholarly journals Evaluation of bacterial hosts for conversion of lignin-derived p-coumaric acid to 4-vinylphenol

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Alberto Rodriguez ◽  
Jamie A. Meadows ◽  
Ning Sun ◽  
Blake A. Simmons ◽  
John M. Gladden
Keyword(s):  
Acid Decarboxylase ◽  
Coumaric Acid ◽  
Batch Cultures ◽  
Extraction And Purification ◽  
Rich Media ◽  
Phenolic Acid Decarboxylase ◽  
High Level ◽  
Level Production ◽  
Substrate Concentrations ◽  
Continuous Product

AbstractHydroxycinnamic acids such as p-coumaric acid (CA) are chemically linked to lignin in grassy biomass with fairly labile ester bonds and therefore represent a straightforward opportunity to extract and valorize lignin components. In this work, we investigated the enzymatic conversion of CA extracted from lignocellulose to 4-vinylphenol (4VP) by expressing a microbial phenolic acid decarboxylase in Corynebacterium glutamicum, Escherichia coli, and Bacillus subtilis. The performance of the recombinant strains was evaluated in response to the substrate concentration in rich medium or a lignin liquor and the addition of an organic overlay to perform a continuous product extraction in batch cultures. We found that using undecanol as an overlay enhanced the 4VP titers under high substrate concentrations, while extracting > 97% of the product from the aqueous phase. C. glutamicum showed the highest tolerance to CA and resulted in the accumulation of up to 187 g/L of 4VP from pure CA in the overlay with a 90% yield when using rich media, or 17 g/L of 4VP with a 73% yield from CA extracted from lignin. These results indicate that C. glutamicum is a suitable host for the high-level production of 4VP and that further bioprocess engineering strategies should be explored to optimize the production, extraction, and purification of 4VP from lignin with this organism.

High level production of human proapo A-I by fed-batch culture of recombinant Escherichia coli

1993 ◽  
Vol 75 (2) ◽  
pp. 155-157 ◽  
Author(s):  
Kunihiko Ohta ◽  
Tatsuro Shibui ◽  
Yuuki Morimoto ◽  
Shinji Iijima ◽  
Takeshi Kobayashi
Keyword(s):  
Escherichia Coli ◽  
Batch Culture ◽  
Recombinant Escherichia Coli ◽  
Fed Batch ◽  
Fed Batch Culture ◽  
High Level ◽  
Level Production

scholarly journals High-Level Production of Human Leptin by Fed-Batch Cultivation of Recombinant Escherichia coli and Its Purification

1999 ◽  
Vol 65 (7) ◽  
pp. 3027-3032 ◽  
Author(s):  
Ki Jun Jeong ◽  
Sang Yup Lee
Keyword(s):  
Escherichia Coli ◽  
Total Protein ◽  
Anion Exchange Chromatography ◽  
Batch Cultivation ◽  
Exchange Chromatography ◽  
Total Protein Content ◽  
Fed Batch ◽  
T7 Promoter ◽  
High Level ◽  
Level Production

ABSTRACT Human leptin is a 16-kDa (146-amino-acid) protein that is secreted from adipocytes and influences body weight homeostasis. In order to obtain high-level production of leptin, the human obesegene coding for leptin was expressed in Escherichia coliBL21(DE3) under the strong inducible T7 promoter. The recombinant leptin was produced as inclusion bodies in E. coli, and the recombinant leptin content was as high as 54% of the total protein content. For production of recombinant human leptin in large amounts, pH-stat fed-batch cultures were grown. Expression of leptin was induced at three different cell optical densities at 600 nm (OD600), 30, 90, and 140. When cells were induced at an OD600 of 90, the amount of leptin produced was 9.7 g/liter (37% of the total protein). After simple purification steps consisting of inclusion body isolation, denaturation and refolding, and anion-exchange chromatography, 144.9 mg of leptin that was more than 90% pure was obtained from a 50-ml culture, and the recovery yield was 41.1%.

High level production of itaconic acid at low pH by Ustilago maydis with fed-batch fermentation

2021 ◽  
Author(s):  
Hatice Taşpınar Demir ◽  
Emine Bezirci ◽  
Johanna Becker ◽  
Hamed Hosseinpour Tehrani ◽  
Emrah Nikerel ◽  
...  
Keyword(s):  
Itaconic Acid ◽  
Batch Fermentation ◽  
Ustilago Maydis ◽  
Low Ph ◽  
Fed Batch ◽  
Fed Batch Fermentation ◽  
High Level ◽  
Level Production

High level production of active streptokinase in Pichia pastoris fed-batch culture

2016 ◽  
Vol 83 ◽  
pp. 50-60 ◽  
Author(s):  
Adivitiya ◽  
Vikas Kumar Dagar ◽  
Nirmala Devi ◽  
Yogender Pal Khasa
Keyword(s):  
Pichia Pastoris ◽  
Batch Culture ◽  
Fed Batch ◽  
Fed Batch Culture ◽  
High Level ◽  
Level Production
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