Stabilization of an amylase from Neurospora crassa by Immobilization on Highly Activated Supports

• Autor(a) principal: Tavano, Olga L.
• Data de Publicação: 2008
• Outros Autores: Pessela, Benevides C. C., Goulart, Antonio J., Fernández-Lafuente, Roberto, Guisán, José M., Monti, Rubens [UNESP]
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNESP
• Texto Completo: http://dx.doi.org/10.1080/08905430802262616; http://hdl.handle.net/11449/225248
• topic: Amylase; Enzyme immobilization; Enzyme stabilization; Glyoxyl agarose; Neurospora crassa

The amylase from Neurospora crassa is an interesting enzyme, having higher stability than amylase from Aspergillus oryzea under a broad range of pH values. Moreover, the N. crassa enzyme may be immobilized on different supports with good retention of enzyme activity. The best stabilizations were achieved using Eupergit C 250 L or glyoxyl agarose, with which the enzyme remained fully active at 60°C for 24 h while the soluble enzyme remained about 17%. The glyoxyl agarose immobilized enzyme had high thermostability, high optimal temperature (65°C) and broad pH/activity profile, suggesting that this enzyme has potential for food and industrial applications for starch modification. Copyright © Taylor & Francis Group, LLC.