Molecular cloning and expression of thermostable glucose-tolerant β-glucosidase of Penicillium funiculosum NCL1 in Pichia pastoris and its characterization

Journal of Industrial Microbiology and Biotechnology

Volumn 42, Issue 4, 2015, Pages 553-565

  Ramani, Gurusamy ^a   Meera, Balasubramanian ^a   Vanitha, Chinnathambi ^a   Rajendhran, Jeyaprakash ^a   Gunasekaran, Paramasamy ^a  

^a MADURAI KAMARAJ UNIVERSITY   (India)

Author keywords

Glucose tolerant; Penicillium funiculosum NCL1; Pichia pastoris; Thermo tolerant; Glucosidase

Indexed keywords

ASPARTIC ACID; BETA GLUCOSIDASE; CALCIUM; CELLOBIOSE; CELLULASE; CYSTEINE; GENOMIC DNA; GLUCOSE; GLUTAMIC ACID; MAGNESIUM; MANGANESE; NITROGEN 13; PHLEOMYCIN; POTASSIUM; RECOMBINANT ENZYME; RECOMBINANT PROTEIN; SODIUM; ZINC; ALCOHOL; CELLULOSE;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME SYNTHESIS; EXON; GENE EXPRESSION; GLUCONEOGENESIS; GLUCOSE TOLERANCE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HINGE REGION; INTRON; KLUYVEROMYCES MARXIANUS; KOMAGATAELLA PASTORIS; MOLECULAR CLONING; NATIVE POLYACRYLAMIDE GEL ELECTROPHORESIS; NONHUMAN; PENICILLIUM PURPUROGENUM; PHYSICAL CHEMISTRY; PROMOTER REGION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SWISS-PROT; TALAROMYCES FUNICULOSUS; THERMOASCUS; ZYMOGRAPHY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYMOLOGY; GENETICS; HYDROLYSIS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; MOLECULAR WEIGHT; PENICILLIUM; PH; PICHIA; SUPPLY AND DISTRIBUTION; TEMPERATURE; TRICHODERMA;

AMINO ACID SEQUENCE; BETA-GLUCOSIDASE; CATALYTIC DOMAIN; CELLOBIOSE; CELLULASE; CELLULOSE; CLONING, MOLECULAR; ENZYME STABILITY; ETHANOL; GLUCOSE; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PENICILLIUM; PICHIA; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TEMPERATURE; TRICHODERMA;

EID: 84925496790     PISSN: 13675435     EISSN: 14765535     Source Type: Journal    
DOI: 10.1007/s10295-014-1549-6     Document Type: Article

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