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Arnold L. Demain
Researcher at Drew University
Publications - 425
Citations - 21576
Arnold L. Demain is an academic researcher from Drew University. The author has contributed to research in topics: Streptomyces clavuligerus & Clostridium thermocellum. The author has an hindex of 66, co-authored 424 publications receiving 20140 citations. Previous affiliations of Arnold L. Demain include Massachusetts Institute of Technology & Merck & Co..
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Manual of Industrial Microbiology and Biotechnology, Third Edition
Lee R. Lynd,Huimin Zhao,Leonard Katz,Richard H. Baltz,Alan T. Bull,Beth Junker,Prakash S. Masurekar,Julian Davies,Christopher D. Reeves,Arnold L. Demain +9 more
Journal ArticleDOI
Aflatoxin B1 mutagenesis, DNA binding, and adduct formation in Salmonella typhimurium
TL;DR: Salmonella typhimurium strain TM677 was mutagenized with aflatoxin B1 in liquid suspension culture in the presence of a rat liver postmitochondrial supernatant and forward mutation to 8-azaguanine resistance was measured in the treated cultures and was found to increase linearly with AFB1 concentration.
Journal ArticleDOI
Regulation of isopenicillin N synthetase and deacetoxycephalosporin C synthetase by carbon source during the fermentation of Cephalosporium acremonium
TL;DR: A strong glucose catabolite repression of the expandase is pointed to as one of the main regulatory mechanisms in β-lactam biosynthesis by Cephalosporium acremonium and the reason for accumulation of penicillin N during the fermentation.
Journal ArticleDOI
Production and antibacterial activity of malforming C, a toxic metabolite of Aspergillus niger.
TL;DR: The production of the new mycotoxin malformin C by a solid substrate fermentation is described and it is shown that this product is highly toxic and exerts antibacterial activity against a variety of gram-positive and gram-negative organisms.
Journal ArticleDOI
Methionine control of cephalosporin C formation
Stephen W. Drew,Arnold L. Demain +1 more
TL;DR: The data strongly indicate that stimulation by methionine is not a function of its ability to donate sulfur for antibiotic formation, and norleucine was found to neither repress nor inhibit cysteine metabolism.