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Immobilization of pectinmethylesterase from acerola (Malpighia glabra L.) in porous silica

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Abstract

The total and partially purified enzyme pectinmethylesterase from acerola fruit was covalently immobilized on porous silica particles. These efficiency values were 114% for the total PME and 351% for the partially purified PME. In both forms the immobilization resulted in compounds with high thermal stability.

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Authors and Affiliations

  1. Departamento de Bioquímica e Tecnologia Química, UNESP, Instituto de Química, Rua Prof. Francisco Degni, s/n. °, C.P. 355, CEP 14801-970, Araraquara, SP, Brasil

    Sandra Aparecida de Assis, Henrique Celso Trevisan, Olga Maria Mascarenhas & Faria Oliveira

Authors
  1. Sandra Aparecida de Assis
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  2. Henrique Celso Trevisan
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  3. Olga Maria Mascarenhas
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  4. Faria Oliveira
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Correspondence to Faria Oliveira.

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Aparecida de Assis, S., Trevisan, H.C., Maria Mascarenhas, O. et al. Immobilization of pectinmethylesterase from acerola (Malpighia glabra L.) in porous silica. Biotechnology Letters 25, 869–872 (2003). https://doi.org/10.1023/A:1024088326346

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  • DOI: https://doi.org/10.1023/A:1024088326346

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