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Category Archives: Biotechnology
Biotechnology – A-Level (A2) Biology Revision – Video
Biotechnology - A-Level (A2) Biology Revision
Biotechnology. A2 Biology. OCR Exam Board. Unit 5.2.2. F215. The "You need to know..." section has come from the OCR specification.
By: ocrbiologya2
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Biotechnology - A-Level (A2) Biology Revision - Video
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Biotechnology Banquet at WestCTA – Video
Biotechnology Banquet at WestCTA
Teaching somethings about the cheese and introducing the raw making of it, no touches at all, just how CHEESE ACTUALLY IS when it #39;s made.
By: Karnevation
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Oliver Byrne – BSc Biotechnology – Video
Oliver Byrne - BSc Biotechnology
Oliver wasn #39;t exactly sure about what he wanted to do when he first started at university, now he #39;s chosen microbiology in plant science. Video by Debs Store...
By: NottmUniversity
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Oliver Byrne - BSc Biotechnology - Video
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Ecomann Biotechnology – Video
Ecomann Biotechnology
Ecomann is a high-tech enterprise specializing in the R D, production, sales and applications of PHA. Ecomann has the completely independent intelligent prop...
By: FantasticPlastics4
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Ecomann Biotechnology - Video
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Conversion of fatty aldehydes into alk (a/e)nes by in vitro reconstituted cyanobacterial aldehyde-deformylating oxygenase with the cognate electron transfer system
Background:
Biosynthesis of fatty alk(a/e)ne in cyanobacteria has been considered as a potential basis for the sunlight-driven and carbon-neutral bioprocess producing advanced solar biofuels. Aldehyde-deformylating oxygenase (ADO) is a key enzyme involved in that pathway. The heterologous or chemical reducing systems were generally used in in vitro ADO activity assay. The cognate electron transfer system from cyanobacteria to support ADO activity is still unknown.
Results:
We identified the potential endogenous reducing system including ferredoxin (Fd) and ferredoxin-NADP+ reductase (FNR) to support ADO activity in Synechococcus elongatus PCC7942. ADO (Synpcc7942_1593), FNR (SynPcc7942_0978), and Fd (SynPcc7942_1499) from PCC7942 were cloned, overexpressed, purified, and characterized. ADO activity was successfully supported with the endogenous electron transfer system, which worked more effectively than the heterologous and chemical ones. The results of the hybrid Fd/FNR reducing systems demonstrated that ADO was selective against Fd. And it was observed that the cognate reducing system produced less H2O2 than the heterologous one by 33% during ADO-catalyzed reactions. Importantly, kcat value of ADO 1593 using the homologous Fd/FNR electron transfer system is 3.7-fold higher than the chemical one.
Conclusions:
The cognate electron transfer system from cyanobacteria to support ADO activity was identified and characterized. For the first time, ADO was functionally in vitro reconstituted with the endogenous reducing system from cyanobacteria, which supported greater activity than the surrogate and chemical ones, and produced less H2O2 than the heterologous one. The identified Fd/FNR electron transfer system will be potentially useful for improving ADO activity and further enhancing the biosynthetic efficiency of hydrocarbon biofuels in cyanobacteria.Source:
http://www.biotechnologyforbiofuels.com/content/6/1/86
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2013 AAPS National Biotechnology Conference – Video
2013 AAPS National Biotechnology Conference
Perspectives from attendees of the 2013 AAPS National Biotechnology Conference in San Diego, CA May 20-22, 2013.
By: AAPSPharmaceutica
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2013 AAPS National Biotechnology Conference - Video
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