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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..
Papers
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Journal ArticleDOI
Production of recombinant proteins by microbes and higher organisms.
Arnold L. Demain,Preeti Vaishnav +1 more
TL;DR: The most popular system for producing recombinant mammalian glycosylated proteins is that of mammalian cells while transgenic plants such as Arabidopsis thaliana and others can generate many recombinant proteins.
Journal ArticleDOI
Cellulase, Clostridia, and Ethanol
TL;DR: The need for such a process, the cellulases of clostridia, their presence in extracellular complexes or organelles (the cellulosomes), the binding of the cellulosome to cellulose and to the cell surface, cellulase genetics, regulation of their synthesis, cocultures, ethanol tolerance, and metabolic pathway engineering for maximizing ethanol yield are discussed.
Book
Manual of industrial microbiology and biotechnology
Arnold L. Demain,Julian Davies +1 more
TL;DR: The culture The process Strain Improvement Immobilization and Cell Culture Biochemical Engineering Special Topics as discussed by the authors The culture the process strain improvement Immobilisation and cell culture Biochemical engineering
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Microbial drug discovery: 80 years of progress
Arnold L. Demain,Sergio Sánchez +1 more
TL;DR: This review centers on these beneficial secondary metabolites, the discovery of which goes back 80 years to the time when penicillin was discovered by Alexander Fleming.
Journal ArticleDOI
Microbial Enzymes: Tools for Biotechnological Processes
José L. Adrio,Arnold L. Demain +1 more
TL;DR: Microbial diversity and modern molecular techniques are being used to discover new microbial enzymes whose catalytic properties can be improved/modified by different strategies based on rational, semi-rational and random directed evolution.