Multi-site saturation by OmniChange yields a pH- and thermally improved phytase

Journal of Biotechnology

Volumn 170, Issue 1, 2014, Pages 68-72

  Shivange, Amol V ^a,b,c   Dennig, Alexander ^a   Schwaneberg, Ulrich ^a,b  

^a RWTH AACHEN UNIVERSITY   (Germany)

^b JACOBS UNIVERSITY BREMEN   (Germany)

^c University of California   (United States)

Author keywords

Directed evolution; Multiple site saturation; PH stability; Phytase; Protein engineering

Indexed keywords

DIRECTED EVOLUTION; GASTRIC RESIDENCE TIME; HIGH SPECIFIC ACTIVITIES; PH STABILITY; PHYTASES; PROTEIN ENGINEERING; RESIDUAL ACTIVITY; SATURATION MUTAGENESIS;

BIOCHEMICAL ENGINEERING; ENZYMES; INDUSTRIAL APPLICATIONS;

PH EFFECTS;

PHYTASE; UNCLASSIFIED DRUG; YERSINIA MOLLARETII PHYTASE;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL PARAMETERS; HEAT TOLERANCE; HIGH THROUGHPUT SCREENING; HYDROGEN BOND; MELTING POINT; MOLECULAR EVOLUTION; MUTAGENESIS; MUTATION RATE; PH; PH STABILITY; PRIORITY JOURNAL; PROTEIN ENGINEERING; STOP CODON; THERMOSTABILITY;

DIRECTED EVOLUTION; MULTIPLE SITE SATURATION; PH STABILITY; PHYTASE; PROTEIN ENGINEERING;

6-PHYTASE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; ENZYME STABILITY; GENETIC VARIATION; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; SUBSTRATE SPECIFICITY; TEMPERATURE; YERSINIA;

EID: 84890854387     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2013.11.014     Document Type: Article

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