Biotechnology and Applied Biochemistry · 2003 · 46 citations · 23 references
Life SciencesBiochemistryMicrobiologyBacteriologyEnzymologyMicrobial MetabolismEnvironmental Microbial BiotechnologyEnzyme IsolationEnzyme KineticsEnzyme PurificationMicrobial Enzyme ProductionMicrobial GrowthChromatographic Enzyme PurificationEnzyme Affinity PurificationEnzyme Recovery From Crude ExtractsMicrobial Enzyme FunctionMolecular Mass DeterminationOptimum TemperaturePurificationTemperature Optimum
A new microbial transglutaminase (EC 2.3.2.13) from a Bacillus circulans strain isolated from the aquatic Amazonian environment was purified and characterized. Enzyme purification started with (NH(4))(2)SO(4) 'salting out' and proceeded with liquid chromatography on Q-Sepharose FF and octyl-Sepharose 4 FF. The purification factor was approx. 150-fold with a yield of 32%. The enzyme's molecular mass was estimated as 45000 Da on SDS/PAGE. The purified transglutaminase had an optimum temperature of 47 degrees C, the optimum pH of the reaction was 7 and it presented no calcium-dependent activity.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations