Deactivation kinetics and response surface analysis of the stability of α-l-rhamnosidase from Penicillium decumbens

Applied Biochemistry and Biotechnology

Volumn 152, Issue 1, 2009, Pages 29-41

  Magario, I ^a   Neumann, A ^a   Oliveros, E ^a,b   Syldatk, C ^a  

^a UNIVERSITY OF KARLSRUHE   (Germany)

^b Université Paul Sabatier   (France)

Author keywords

Rhamnosidase; Doehlert array; Enzyme stability; Naringinase; Response surface methodology; Series type deactivation kinetics

Indexed keywords

DOEHLERT ARRAY; ENZYME STABILITY; NARINGINASE; RESPONSE SURFACE METHODOLOGY; SERIES-TYPE DEACTIVATION KINETICS;

CARBOHYDRATES; DIGESTIVE SYSTEM; ENZYMES; PH EFFECTS; RATE CONSTANTS; STABILITY; SURFACE ANALYSIS; SURFACE PROPERTIES; ULTRAFILTRATION;

ENZYME ACTIVITY;

ALPHA LEVO RHAMNOSIDASE; BETA GLUCOSIDASE; DEXTRAN; GLYCOSIDASE; NARINGINASE; UNCLASSIFIED DRUG; ALPHA L RHAMNOSIDASE; ALPHA-L-RHAMNOSIDASE; GLYCOLIPID; MULTIENZYME COMPLEX; RHAMNOLIPID;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME STABILITY; NONHUMAN; PENICILLIUM; PENICILLIUM DECUMBENS; PH; RESPONSE SURFACE METHOD; TEMPERATURE DEPENDENCE; THERMOSTABILITY; BIOLOGICAL MODEL; CHEMISTRY; DRUG EFFECT; ENZYME ACTIVATION; ENZYMOLOGY; KINETICS; METABOLISM; TEMPERATURE;

PENICILLIUM DECUMBENS;

BETA-GLUCOSIDASE; ENZYME ACTIVATION; ENZYME STABILITY; GLYCOLIPIDS; GLYCOSIDE HYDROLASES; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, BIOLOGICAL; MULTIENZYME COMPLEXES; PENICILLIUM; TEMPERATURE;

EID: 59649092702     PISSN: 02732289     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12010-008-8204-5     Document Type: Article

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