Studies on the Adsorption of Inulinase from Kluyveromyces marxianus ATCC 16045 onto an Ion Exchange Resin

• Autor(a) principal: Kalil, Susana Juliano
• Data de Publicação: 2006
• Outros Autores: Pasotto, Marlei Barboza, Maugeri Filho, Francisco, Rodrigues, Maria Isabel
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da FURG (RI FURG)
• Texto Completo: http://repositorio.furg.br/handle/1/4698
• topic: Inulinase; Streamline; Purification; Kluyveromyces; Ion Exchange Inulinase; Purificação; Troca iônica

The adsorption of an extracellular inulinase directly onto an ion exchange resin from a clarified crude broth was investigated in this work. The enzyme inulinase was obtained from Kluyveromyces marxianus ATCC 16045 by fermentation in shaken flasks in a medium containing peptone, sucrose, yeast extract and K2HPO4 at pH 3.5, 30°C and 150 rpm for 48 hours. The final enzymatic activity was about 72 U mL–1. The crude broth filtrate was used for kinetic studies and for the adsorption isotherm of the extracellular inulinase from Kluyveromyces bulgaricus ATCC 16045 onto an ion exchange resin. The trials were carried out at pH 3.5 and 25°C in stirred tank reactors containing STREAMLINETM SP, developed for expanded bed adsorption. It was observed that the adsorption was well described by the Langmuir isotherm, and the values determined for Qm and Kd were 1,254 U mL–1 and 0.325 UmL–1, respectively. The kinetic parameters k1 (6.52 . 10–3 mL U–1 min) and k2 (2.09. 10–3 min–1) as well as the average values of 1.71 . 10–2 cm s–1 for the film coefficient (Ks) and 6.96 . 10–7 cm2 s–1 for the effective diffusion coefficient (Def), were determined using the experimental results and mathematical modelling.