Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: Factors contributing to increased activity retention

Protein Science

Volumn 21, Issue 4, 2012, Pages 487-497

  Augustyniak, Wojciech ^a   Brzezinska, Agnieszka A ^a   Pijning, Tjaard ^b   Wienk, Hans ^c   Boelens, Rolf ^c   Dijkstra, Bauke W ^b   Reetz, Manfred T ^a,d  

^a MAX PLANCK INSTITUT FÜR KOHLENFORSCHUNG   (Germany)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

^c UTRECHT UNIVERSITY   (Netherlands)

^d PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

Aggregation; Directed evolution; Iterative saturation mutagenesis; Lipase; Thermal inactivation

Indexed keywords

ACID LIPASE; AMINO ACID; BACTERIAL ENZYME; MEMBRANE PROTEIN; MUTANT PROTEIN;

ARTICLE; BACILLUS SUBTILIS; CIRCULAR DICHROISM; CONTROLLED STUDY; COOLING; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME STRUCTURE; IN VITRO STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRECIPITATION; PRIORITY JOURNAL; PROTEIN UNFOLDING; RANDOMIZATION; STRUCTURE ANALYSIS; TEMPERATURE STRESS; THERMOSTABILITY; X RAY ANALYSIS;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; BINDING SITES; BIOPHYSICAL PROCESSES; CHEMICAL PRECIPITATION; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; HOT TEMPERATURE; LIPASE; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; PLASMIDS; PROTEIN DENATURATION; STRESS, PHYSIOLOGICAL;

BACILLUS SUBTILIS;

EID: 84858689964     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2031     Document Type: Article

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