Purification strategies, characteristics and thermodynamic analysis of a highly thermostable alkaline protease from a salt-tolerant alkaliphilic actinomycete, Nocardiopsis alba OK-5

Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences

Volumn 889-890, Issue , 2012, Pages 61-68

  Gohel, Sangeeta D ^a   Singh, Satya P ^a  

^a SAURASHTRA UNIVERSITY   (India)

Author keywords

Alkaline protease; Denaturation constant; Enzyme kinetics; Enzyme purification; Salt tolerant alkaliphilic actinomycetes; Thermodynamics; Thermostability

Indexed keywords

ALKALINE PROTEASE; ALKALIPHILIC; CHEMICAL DENATURATION; DEACTIVATION RATE; ENZYME PURIFICATION; HALF LIVES; HYDROPHOBIC INTERACTIONS; MERCAPTOETHANOL; NOCARDIOPSIS; ONE-STEP METHODS; PURIFICATION METHOD; SALT TOLERANT; THERMO DYNAMIC ANALYSIS; THERMOSTABILITY;

ACTIVATION ENERGY; AMINO ACIDS; BACTERIA; ENZYME KINETICS; METAL IONS; PURIFICATION; RATE CONSTANTS; SODIUM CHLORIDE; SURFACE ACTIVE AGENTS; THERMOANALYSIS; THERMODYNAMICS;

ALKALINITY;

ALKALINE PROTEINASE; BACTERIAL ENZYME; ELECTROLYTE; GLUTAMATE SODIUM; MERCAPTOETHANOL; METAL ION; OXIDIZING AGENT; REDUCING AGENT; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SODIUM CHLORIDE; SURFACTANT;

ACTINOBACTERIA; ARTICLE; BACTERIAL STRAIN; CONTROLLED STUDY; ENTHALPY; ENTROPY; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STABILITY; HALF LIFE TIME; HYDROLYSIS; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; MOLECULAR WEIGHT; NOCARDIOPSIS ALBA; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PHYLOGENETIC TREE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; TEMPERATURE; THERMODYNAMICS;

ACTINOBACTERIA; BACTERIAL PROTEINS; CHROMATOGRAPHY, ION EXCHANGE; ENDOPEPTIDASES; ENZYME STABILITY; KINETICS; PHYLOGENY; SALT-TOLERANCE; SODIUM CHLORIDE; SODIUM GLUTAMATE; SURFACE-ACTIVE AGENTS; THERMODYNAMICS;

ACTINOBACTERIA (CLASS); NOCARDIOPSIS ALBA;

EID: 84862829109     PISSN: 15700232     EISSN: 1873376X     Source Type: Journal    
DOI: 10.1016/j.jchromb.2012.01.031     Document Type: Article

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