Biochemical and enzymatic properties of a fibrinolytic enzyme from Pleurotus eryngii cultivated under solid-state conditions using corn cob

Bioresource Technology

Volumn 101, Issue 16, 2010, Pages 6475-6481

  Cha, Wol Suk ^a   Park, Sang Shin ^b   Kim, Sung Jin ^a   Choi, DuBok ^a,c  

^a Chosun University   (South Korea)

^b Dongguk University   (South Korea)

^c Chodang University   (South Korea)

Author keywords

Corn cob; Fibrinolytic enzyme; Pleurotus eryngii; Serine protease

Indexed keywords

AMINO ACIDS; CHAINS; DRUG THERAPY; ENZYMES; GENE ENCODING;

CORN COB; ENZYMATIC PROPERTIES; FIBRINOLYTIC ENZYMES; N-TERMINAL SEQUENCES; PHENYLMETHYLSULFONYL FLUORIDE; PLEUROTUS ERYNGII; SERINE PROTEASE; THROMBOLYTIC THERAPIES;

ENZYME ACTIVITY;

ALANYLMETHIONYLASPARTYLSERYLGLUTAMINYLTHREONYLASPARTYLALANYLSERYLTYROSYLGLYCYLLEUCYLALANYLASPARAGINYLASPARTIC ACID; BENZYLSULFONYL FLUORIDE; CATHEPSIN G; ELASTASE; FIBRINOGEN; FUNGAL ENZYME; KALLIKREIN; PEPTIDE DERIVATIVE; PLASMIN; SERINE PROTEINASE; SUBTILISIN; THROMBIN; UNCLASSIFIED DRUG; ENZYME; ENZYME INHIBITOR;

BIOCHEMICAL COMPOSITION; ELECTROKINESIS; ENZYME ACTIVITY; FUNGUS; HYDROLYSIS; PH; SUBSTRATE; THROMBOLITE;

ALPHA CHAIN; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BETA CHAIN; CHEMICAL ANALYSIS; COMPETITIVE INHIBITION; CORN; ENERGY RESOURCE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME SUBSTRATE; FIBRINOLYSIS; FIBRINOLYTIC THERAPY; FRUITING BODY; INCUBATION TIME; MOLECULAR WEIGHT; NONHUMAN; PH; PLEUROTUS; PLEUROTUS ERYNGII; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; SEQUENCE ANALYSIS; SOLID STATE FERMENTATION; SPECIES CULTIVATION; CHEMISTRY; ENZYMOLOGY; MAIZE; METABOLISM; MOLECULAR GENETICS; SEQUENCE HOMOLOGY;

PLEUROTUS ERYNGII; ZEA MAYS;

AMINO ACID SEQUENCE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; ENZYMES; FIBRINOLYSIS; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PHENYLMETHYLSULFONYL FLUORIDE; PLEUROTUS; SEQUENCE HOMOLOGY, AMINO ACID; ZEA MAYS;

EID: 77955476618     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2010.02.048     Document Type: Article

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