A novel endo-1,4-β-mannanase from Bispora antennata with good adaptation and stability over a broad pH range

Applied Biochemistry and Biotechnology

Volumn 166, Issue 6, 2012, Pages 1442-1453

  Liu, Qiong ^a   Yang, Peilong ^a   Luo, Huiying ^a   Shi, Pengjun ^a   Huang, Huoqing ^a   Meng, Kun ^a   Yao, Bin ^a  

^a INSTITUTE OF PLANT PROTECTION   (China)

Author keywords

mannanase; Bispora antennata; pH adaptation and stability

Indexed keywords

ALKALINE CONDITIONS; AMINO ACID SEQUENCE; ASPERGILLUS ACULEATUS; BASE PAIRS; BISPORA ANTENNATA; CHEMICAL REAGENTS; COLLAGENASE; ELECTROPHORETIC HOMOGENEITY; ENCODING GENES; FOOD INDUSTRIES; GLYCOSIDE HYDROLASES; LOCUST BEAN GUM; MANNANASE; MERCAPTOETHANOL; NEUTRAL PROTEASE; OPTIMAL ACTIVITY; PH RANGE; PH VALUE; PICHIA PASTORIS; PROTEINASE K; SPECIFIC ACTIVITY; SUBTILISIN;

AMINO ACIDS; CLONING; ENZYME ACTIVITY; INDICATORS (CHEMICAL); METAL IONS; PH;

ALKALINITY;

ALGAROBA; AMINO ACID; BETA MANNOSIDASE; CHYMOTRYPSIN A; COLLAGENASE; COPPER ION; GLYCOSIDASE; MERCAPTOETHANOL; METAL ION; PROTEINASE K; SUBTILISIN; TRYPSIN;

ACIDITY; ALKALINITY; AMINO ACID SEQUENCE; ARTICLE; ASPERGILLUS; BASE PAIRING; BISPORA ANTENNATA; CONTROLLED STUDY; DEGLYCOSYLATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME STRUCTURE; FLOUR; FUNGUS; HYDROLYSIS; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PICHIA PASTORIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; AMORPHOPHALLUS; ASCOMYCOTA; CATALYTIC DOMAIN; CLONING, MOLECULAR; DNA, COMPLEMENTARY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME ACTIVATION; ENZYME ASSAYS; ENZYME STABILITY; FAGUS; GALACTANS; GENES, FUNGAL; HYDROGEN-ION CONCENTRATION; MANNANS; MANNOSIDASES; MERCAPTOETHANOL; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PEPTIDE HYDROLASES; PICHIA; PLANT GUMS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

ASPERGILLUS ACULEATUS; BISPORA; FAGUS; PICHIA PASTORIS;

EID: 84862823396     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-011-9537-z     Document Type: Article

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