By M.R. El-Gewely
The Biotechnology Annual Review sequence goals at overlaying advancements within the box of biotechnology within the kind of complete, illustrated and well-referenced stories. contemporary enlargement during this box, either commercial and academic, besides the rise within the variety of new journals reporting new effects, has enormously elevated the necessity for precisely this sort of sequence, regularly delivering reviews.
Every quantity, released every year, will disguise a distinct element of biotechnology.
The "Editorial Board" of Biotechnology Annual Review encourages feedback and contributions of articles from or from educational associations that may represent a finished masking of a appropriate subject in biotechnology.
Proposals for contributions and/or feedback for subject matters for destiny volumes during this sequence may be despatched to the Editor:
Professor M.R. El-Gewely division of biotechnology collage of Tromsø IMB, MH-Bygget N-9037 Tromsø Norway Tel: (+47) seventy seven 644654 Fax: (+47) seventy seven 645350
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Additional info for Biotechnology Annual Review, Volume 2, Volume 2
Despite thermozymes being significantly more rigid than their mesophilic counterparts at room temperature [ 1861, increased rigidity at low temperatures and linear Arrhenius behavior are still general mechanisms affecting all enzyme categories. Rigidity is an essential factor in protein thermostability. , at higher temperatures) than mesozymes, thermozymes need to be more rigid than mesozymes. Their higher rigidity is essential for preserving their catalytic active structure, and protects them from unfolding.
Coli mutants . The absence of sequences recognizable as E. coli promoters has made cloning of Therrnus genes difficult. A typical example was the cloning of T . aquaticus Taq DNA polymerase . Most Therrnus genes were expressed in E. coli as fusion genes (T. aquaticus L-lactate dehydrogenase) or fusion proteins (Taq1 restriction endonuclease) (reviewed in ). Koyama and Furukawa (1990)  cloned the T. therrnophilus tryptophan synthase genes by direct plasmid transfer of a genomic library from E.
100 Temperature for maximal activity (“C) Fig. I. Number of asparagine + glutamine residues per xylose isomerase monomer as a function of the temperature for maximal enzyme activity. maximal activity . Despite the small number of enzymes plotted, Fig. 1 clearly shows an inverse relationship between Asn + Gln content and temperature for maximal activity. More information is needed on proteins from thermophiles and hyperthermophiles to confirm this trend in a statistically significant way. Contrary to the early belief that thermophilic enzymes gained their thermostability from a different amino acid composition, enzyme thermostability is enhanced by numerous subtle sequence differences.