Protein and Amino Acid Metabolism of Thermoanaerobacter mathranii
The members within the genus Thermoanerobacter have been much less investigated for protein and amino acid metabolism as compared with carbohydrates. The present study investigates the biotechnological potential of Thermoanaerobacter mathranii (DSM 11426) concerning its ability to produce high energy alcohols from amino and fatty acids.
Jóhann Orlygsson +2 more
openaire +1 more source
Biologically induced mineralization by bacteria [PDF]
Minerali formirani biološki induciranim procesom mineralizacije tvore jezgru i rastu izvan stanice kao rezultat metaboličke aktivnosti organizma i kasnijih kemijskih reakcija koje uključuju produkte metabolizma.
Vlah, Tamara
core +2 more sources
Thermoanaerobacter kivui is the thermophilic acetogenic bacterium with the highest temperature optimum (66°C) and with high growth rates on hydrogen (H2) plus carbon dioxide (CO2).
Christoph Baum +5 more
doaj +1 more source
Thermostable lipases from the extreme thermophilic anaerobic bacteria Thermoanaerobacter thermohydrosulfuricus SOL1 and Caldanaerobacter subterraneus subsp. tengcongensis [PDF]
Marina Royter +6 more
core +1 more source
Metabolic Engineering of Ethanol Production in Thermoanaerobacter mathranii BG1 [PDF]
Yao, Shuo
core
Optimization of bioethanol production from carbohydrate rich wastes by extreme thermophilic microorganisms [PDF]
Tomás, Ana Faria
core
Amino Acid and Related Catabolism of Thermoanaerobacter Species
Sá hluti lífeðlisfræði hitakærra baktería sem snýr að prótein- og amínósýruefnaskiptum hefur að mestu verið vanræktur í gegnum tíðina þrátt fyrir möguleika sem í þeim felast á sviði líftækni. Við loftfirrðar aðstæður krefjast margar próteinmyndandi amínósýrur utanaðkomandi rafeindaþega til þess að úr verði orkufræðilega hagstæðar aðstæður fyrir ...
openaire +1 more source
Use of a newly isolated extreme thermophile for the production of 2nd generation bio-ethanol [PDF]
Angelidaki, Irini +3 more
core
The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog [PDF]
Matthew J Cuneo +4 more
core +1 more source

