Stability and structural changes of horseradish peroxidase: Microwave versus conventional heating treatment

Enzyme and Microbial Technology

Volumn 69, Issue , 2015, Pages 10-18

  Lopes, Lucas C ^a   Barreto, Maria T M ^a   Gonçalves, Karen M ^b   Alvarez, Heiddy M ^c   Heredia, Montserrat Fortuny ^a   de Souza, Rodrigo Octavio M A ^b   Cordeiro, Yraima ^b   Dariva, Cláudio ^a   Fricks, Alini T ^a  

^a TIRADENTES UNIVERSITY   (Brazil)

^b FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^c DEPARTAMENTO DE CIÊNCIAS BIOLÓGICAS   (Brazil)

Author keywords

Conventional heating; Far UV circular dichroism; Horseradish peroxidase; Microwave; Residual activity; Tryptophan fluorescence spectroscopy

Indexed keywords

AMINO ACIDS; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; FOOD PRODUCTS; MICROWAVES;

CONFORMATIONAL CHANGE; CONVENTIONAL HEATING; HORSE-RADISH PEROXIDASE; INTRINSIC FLUORESCENCE; RESIDUAL ACTIVITY; SECONDARY AND TERTIARY STRUCTURES; STRUCTURE AND ACTIVITIES; TERTIARY STRUCTURES;

ENZYME ACTIVITY;

BUFFER; HORSERADISH PEROXIDASE; TRYPTOPHAN;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE SPECTROSCOPY; HEATING; MICROWAVE RADIATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; THERMOSTABILITY; ANTAGONISTS AND INHIBITORS; CHEMISTRY; HEAT; METABOLISM; PROTEIN TERTIARY STRUCTURE;

ARMORACIA RUSTICANA;

CIRCULAR DICHROISM; ENZYME STABILITY; HORSERADISH PEROXIDASE; HOT TEMPERATURE; MICROWAVES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; TRYPTOPHAN;

EID: 84914166663     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2014.11.002     Document Type: Article

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