Purification step of recombinant DAEase produced using the optimized auto-induction method in chemically defined medium containing 1.5% lactose, 0.125% glucose and 1.5% glycerol at 37 <sup>◦</sup>C.

Purification step of recombinant DAEase produced using the optimized auto-induction method in chemically defined medium containing 1.5% lactose, 0.125% glucose and 1.5% glycerol at 37 <sup>◦</sup>C.

<p>Purification step of recombinant DAEase produced using the optimized auto-induction method in chemically defined medium containing 1.5% lactose, 0.125% glucose and 1.5% glycerol at 37 <sup>◦</sup>C.</p>

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Détails bibliographiques
Auteur principal:	Kenny Lischer (21688679) (author)
Autres auteurs:	Fina Amreta Laksmi (14793542) (author), Yudhi Nugraha (21688682) (author), Fauziah Az-Zahra (21688685) (author), David Herawan (21688688) (author), Ario Betha Juanssilfero (21688691) (author), Des Saputro Wibowo (21688694) (author), Kharisma Panji Ramadhan (21688697) (author), Isa Nuryana (14793530) (author), Mohd Shukuri Mohamad Ali (3142038) (author)
Publié:	2025
Sujets:	Biochemistry Microbiology Pharmacology Biotechnology Evolutionary Biology Ecology Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified possible health advantages meet industrial demands escherichia coli </ chemically defined media bl21 star ™ 300 rpm agitation 2 vvm aeration scale optimization yielded research work aims based strategy demonstrated key enzyme catalyzing scalable production method fermentor cultures suitable div >< p 5 %, respectively 5 %, 0 enzyme assays confirmed 125 %, work focused scale production induction strategy substitute sucrose specific activity sevenfold increase rare sugar overall yield optimal concentration natural inducer maximum expression maximum amount hplc analysis host expression enhanced reproducibility effective manner catalytic activity 43 mg
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