Native expression and purification of hormone-sensitive lipase from Psychrobacter sp. TA144 enhances protein stability and activity

Biochemical and Biophysical Research Communications

Volumn 420, Issue 3, 2012, Pages 542-546

  Ascione, Giuseppina ^a   de Pascale, Donatella ^b   De Santi, Concetta ^b   Pedone, Carlo ^a   Dathan, Nina Alayne ^a   Monti, Simona Maria ^a  

^a CNR   (Italy)

^b INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

Benzyl alcohol; Lipase; Molecular chaperones; Protein stability; Psychrophile; Trehalose

Indexed keywords

BACTERIAL PROTEIN; BENZYL ALCOHOL; CHAPERONE; HORMONE SENSITIVE LIPASE; RECOMBINANT PROTEIN; SODIUM CHLORIDE; TREHALOSE;

ANIMAL CELL; ARTICLE; BACTERIAL STRAIN; BACTERIUM CULTURE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CULTURE MEDIUM; DISPERSION; ENZYME ACTIVITY; ESCHERICHIA COLI; HIGH TEMPERATURE; MEMBRANE FLUIDITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PSYCHROBACTER;

CIRCULAR DICHROISM; ENZYME STABILITY; ESCHERICHIA COLI; LIGHT; PROTEIN STRUCTURE, SECONDARY; PSYCHROBACTER; RECOMBINANT PROTEINS; SCATTERING, RADIATION; SOLUBILITY; STEROL ESTERASE; TREHALOSE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PSYCHROBACTER; PSYCHROBACTER SP.;

EID: 84859597494     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.03.028     Document Type: Article

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