Physiological and biochemical characterization of the two α-L-rhamnosidases of Lactobacillus plantarum NCC245

Microbiology

Volumn 155, Issue 8, 2009, Pages 2739-2749

  Avila, Marta ^a   Jaquet, Muriel ^b   Moine, Deborah ^b   Requena, Teresa ^a   Peláez, Carmen ^a   Arigoni, Fabrizio ^b   Jankovic, Ivana ^b  

^a INSTITUTO DEL FRÍO CSIC   (Spain)

^b NESTLÉ RESEARCH CENTER   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LEVO RHAMNOSIDASE B1; ALPHA LEVO RHAMNOSIDASE B2; AURANTIIN; BACTERIAL ENZYME; CARBON; GLUCOSE; HESPERETIN; HESPERIDIN; PERMEASE; RHAMNOSE; RUTOSIDE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GROWTH; BACTERIAL STRAIN; CARBON SOURCE; CONTROLLED STUDY; DOWN REGULATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CHEMISTRY; ENZYME INDUCTION; ENZYME REGULATION; ENZYME REPRESSION; ENZYME SUBSTRATE; ESCHERICHIA COLI; GENE OVEREXPRESSION; LACTOBACILLUS PLANTARUM; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; PH; PRIORITY JOURNAL; PROTEIN CARBOHYDRATE INTERACTION; TEMPERATURE SENSITIVITY; TRANSCRIPTION REGULATION; UPREGULATION;

BASE SEQUENCE; CLONING, MOLECULAR; DNA, BACTERIAL; GLUCOSE; GLUCOSIDES; GLYCOSIDE HYDROLASES; HESPERIDIN; LACTOBACILLUS PLANTARUM; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS, DNA; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; LACTOBACILLUS PLANTARUM;

EID: 69949152234     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.027789-0     Document Type: Article

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