Prevention of Protein Denaturation during Exposure to Sterilization Temperatures

Firefly luciferase exposed to a temperature of 135°C for 36 hours retained up to 40 percent of its original activity. Prerequisites for heat stability were the use of a molecular sieve (Sephadex G-25 or Biogel P-300) and a high vacuum (5 $\times $ 10$^{-4}$ mm-Hg). These studies present a possible s...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1967-03, Vol.155 (3767), p.1287-1288
Hauptverfasser:	Chappelle, Emmett W., Rich, Edward, MacLeod, Norman H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Absorbents Adenosine Triphosphate Biopolymer denaturation Cellulose - pharmacology Dextrans Dextrans - pharmacology Enzymes Gels Gels - pharmacology High vacuum Hot Temperature Hydrogen bonds Insecta Luciferases Molecular weight Molecules Protein Denaturation - drug effects Serum Albumin - pharmacology Sterilization
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Beschreibung
Zusammenfassung:	Firefly luciferase exposed to a temperature of 135°C for 36 hours retained up to 40 percent of its original activity. Prerequisites for heat stability were the use of a molecular sieve (Sephadex G-25 or Biogel P-300) and a high vacuum (5 $\times $ 10$^{-4}$ mm-Hg). These studies present a possible solution to the problem of sterilization for exobiological experiments.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.155.3767.1287