Fed-batch production ofThermomonospora fusca endoglucanase by recombinantStreptomyces lividans

Kim, Eunki; Shin, Dong‐Hoon; Irwin, Diana C.; Wilson, David B.

doi:10.1002/(sici)1097-0290(19981005)60:1<70::aid-bit8>3.0.co;2-y

Cited by 9 publications

(8 citation statements)

References 29 publications

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“…Because cell growth is slower but not arrested under these conditions, excess carbon source and/or low pH in the medium differentially affect the biosynthesis/ export of secretory proteins. In contrast to previous observations (Kim et al, 1998), fed-batch introduction of the dextrose did not alleviate suppressed growth (data not shown).…”

Section: Growth Time-course Studies and The Effect Of Dextrosecontrasting

confidence: 99%

“…1, 2). This was particularly prominent in the presence of excess carbon source known to cause medium acidification (DelaCruz et al, 1992;Kim et al, 1998;Madden et al, 1996). Using the anti-mTNF␣ antibody we did observe accumulation of mTNF␣ intracellularly in acidified medium (data not shown).…”

Section: Discussionmentioning

confidence: 87%

“…This would suggest that acidification may, at least in part, influence the protein-secretion pathway. Excess glucose or batch addition of large amounts of nutrients inhibits secretion but not biosynthesis of bacterial and fungal enzymes from Streptomyces (DelaCruz et al, 1992;Kim et al, 1998;Parro and Mellado, 1994). Secretion may be affected by the level (Oh and Liao, 2000) or activity of SecA, the only translocase subunit whose biosynthesis is regulated (Economou, 1998) and by the activities of the four signal peptidases (Lammertyn and Parro et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…In this period of time the pH of the culture was found to increase steadily from an initial value of 7.0 to a final value of 9.5 after 9 d of growth. Final yield of secreted mTNF␣ in this period of time can be significantly increased by addition of exogenous carbon source known to affect production of other heterologous proteins (Kim et al, 1998;Parro and Mellado, 1994). Addition of dextrose at different concen- trations of up to 10 g/L led to a significant increase in the amount of secreted mTNF␣ (Fig.…”

Section: Growth Time-course Studies and The Effect Of Dextrosementioning

confidence: 92%

See 3 more Smart Citations

Protein secretion biotechnology usingStreptomyces lividans: Large-scale production of functional trimeric tumor necrosis factor ?

Pozidis

Lammertyn

Politou

et al. 2001

Biotechnol. Bioeng.

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We evaluated the feasibility of large‐scale production of biopharmaceuticals expressed as heterologous polypeptides from the Gram‐positive bacterium Streptomyces lividans. As a model protein we used murine tumor necrosis factor alpha (mTNFα). mTNFα fused C‐terminally to the secretory signal peptide of the subtilisin‐inhibitor protein from Streptomyces venezuelae. Under appropriate fermentation conditions, significant amounts of mature mTNFα (80–120 mg/L) can be recovered from spent growth media. Efficient downstream processing allowing rapid purification of mTNFα from culture supernatants was developed. Importantly, the protein is recovered from the spent growth medium in its native trimeric state as judged by biophysical analysis. Further, mTNFα secreted by S. lividans is significantly more active in an in vitro apoptosis tissue culture assay than a corresponding polypeptide produced in Escherichia coli. This pilot study provides the first validation of S. lividans protein secretion as an alternative bioprocess for large‐scale production of oligomeric proteins of potential therapeutic value. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 72: 611–619, 2001.

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Section: Growth Time-course Studies and The Effect Of Dextrosecontrasting

confidence: 99%

Section: Discussionmentioning

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Growth Time-course Studies and The Effect Of Dextrosementioning

confidence: 92%

See 2 more Smart Citations

Protein secretion biotechnology usingStreptomyces lividans: Large-scale production of functional trimeric tumor necrosis factor ?

Pozidis

Lammertyn

Politou

et al. 2001

Biotechnol. Bioeng.

View full text Add to dashboard Cite

show abstract

“…Various nitrogen sources were proved to have different influences on carbohydrate degradation [28][29][30][31][32][33][34][35]. In this study, the presence of yeast extract, tryptone, or peptone in the culture medium enhanced cellulase activities more compared with inorganic nitrogen sources as shown in Table 1.…”

Section: Medium Optimizationmentioning

confidence: 88%

Optimization of Growth Medium and Enzyme Assay Conditions for Crude Cellulases Produced by a Novel Thermophilic and Cellulolytic Bacterium, Anoxybacillus sp. 527

Liang

Feng

Yesuf

et al. 2009

Appl Biochem Biotechnol

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A newly isolated Anoxybacillus sp. 527 was found to grow on crystalline cellulose as sole carbon and energy sources. Cellulases secreted by strain 527 were better induced by cellobiose, followed by glucose, lactose, sucrose, and cellulose. Cellulase secretion was enhanced by an optimized medium. Cellulase activity was increased by the addition of Ca(2+) and NH (4) (+) and achieved maximum as 7.0 FPU ml(-1) at 70 degrees C and pH 6.0. Even at 100 degrees C, the enzymes were still active, which implies their potential application in large-scale cellulose conversion process.

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Protein secretion biotechnology using Streptomyces lividans: Large‐scale production of functional trimeric tumor necrosis factor α

Pozidis

Lammertyn

Politou

et al. 2001

Biotechnol. Bioeng.

View full text Add to dashboard Cite

We evaluated the feasibility of large-scale production of biopharmaceuticals expressed as heterologous polypeptides from the Gram-positive bacterium Streptomyces lividans. As a model protein we used murine tumor necrosis factor alpha (mTNFalpha). mTNFalpha fused C-terminally to the secretory signal peptide of the subtilisin-inhibitor protein from Streptomyces venezuelae. Under appropriate fermentation conditions, significant amounts of mature mTNFalpha (80-120 mg/L) can be recovered from spent growth media. Efficient downstream processing allowing rapid purification of mTNFalpha from culture supernatants was developed. Importantly, the protein is recovered from the spent growth medium in its native trimeric state as judged by biophysical analysis. Further, mTNFalpha secreted by S. lividans is significantly more active in an in vitro apoptosis tissue culture assay than a corresponding polypeptide produced in Escherichia coli. This pilot study provides the first validation of S. lividans protein secretion as an alternative bioprocess for large-scale production of oligomeric proteins of potential therapeutic value.

show abstract

Fed-batch production ofThermomonospora fusca endoglucanase by recombinantStreptomyces lividans

Cited by 9 publications

References 29 publications

Protein secretion biotechnology usingStreptomyces lividans: Large-scale production of functional trimeric tumor necrosis factor ?

Protein secretion biotechnology usingStreptomyces lividans: Large-scale production of functional trimeric tumor necrosis factor ?

Optimization of Growth Medium and Enzyme Assay Conditions for Crude Cellulases Produced by a Novel Thermophilic and Cellulolytic Bacterium, Anoxybacillus sp. 527

Protein secretion biotechnology using Streptomyces lividans: Large‐scale production of functional trimeric tumor necrosis factor α

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