Engineering of a metagenome derived lipase toward thermal tolerance: Effect of asparagine to lysine mutation on the protein surface

Gene

Volumn 491, Issue 2, 2012, Pages 264-271

  Sharma, Pushpender Kumar ^a,b   Kumar, Rajender ^c   Kumar, Rakesh ^a   Mohammad, Owais ^d   Singh, Ranvir ^a   Kaur, Jagdeep ^a  

^a PANJAB UNIVERSITY   (India)

^b INDIAN INSTITUTE OF SCIENCE EDUCATION AND RESEARCH MOHALI   (India)

^c NATIONAL INSTITUTE OF PHARMACEUTICAL EDUCATION AND RESEARCH NIPER   (India)

^d ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Catalytic efficiency; Directed evolution; Far UV CD; Fluorescence; Lipase; Mutation

Indexed keywords

ASPARAGINE; DNA; HYDROGEN; LYSINE; TRIACYLGLYCEROL LIPASE; TRYPTOPHAN;

ARTICLE; BIOCHEMISTRY; CATALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STABILITY; FLUORESCENCE SPECTROSCOPY; GENE MUTATION; GENETIC ENGINEERING; HEAT TOLERANCE; HYDROGEN BOND; METAGENOME; METAGENOMICS; MOLECULAR INTERACTION; MOLECULAR MODEL; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SURFACE PROPERTY; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; ANIMALS; ASPARAGINE; CIRCULAR DICHROISM; ENZYME STABILITY; LIPASE; LYSINE; METAGENOME; PROTEIN CONFORMATION; PROTEIN FOLDING; TEMPERATURE;

EID: 81455154019     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2011.09.028     Document Type: Article

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