Peroxidase from peach fruit: thermal Stability

A peroxidase de pessego foi purificada 28,9 vezes por cromatografia de DEAE-celulose, Sephadex G-100 e hidroxiapatite. A enzima purificada mostrou um unico pico de atividade apresentando pH otimo de 5,0 e temperatura de 40oC. A energia de ativacao para a reacao foi 7,97 kcal/mol. A enzima mostrou-se termolabil na faixa de 60 a 80 oC, e com uma inativacao rapida a 80 oC. A eletroforese em gel de poliacrilamida do transcurso da inativacao a 70 oC mostrou uma so banda de atividade. Diferentes tipos de acucares aumentaram a estabilidade termica da atividade enzimatica, na seguinte ordem: sacarose> lactose>glicose>frutose. Medida da atividade residual mostrou um efeito estabilizante da sacarose a varias relacoes temperatura/concentracao (10 a 40%, p/p). A energia de ativacao para inativacao aumentou com aumento crescente da concentracao de sacarose de 0-20% (p/p). Apos inativacao a 70 oC e 75 oC a enzima foi capaz de ser reativada ate 40% da atividade inicial quando armazenada a 30 oC

• Publication year

  1998

• Venue

  Brazilian Archives of Biology and Technology

• Publication date

  Unknown publication date

• Fields of study

  Not labeled

• Identifiers
  DOI 10.1590/S1516-89131998000200002
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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