Immobilisation of endoinulinase on polyhydroxybutyrate microfibers

Abstract

Beran M., Pinkrová J., Urban M., Drahorád J. (2016): Immobilisation of endoinulinase on polyhydroxybutyrate microfibres. Czech J. Food Sci., 34: 541-546.Due to the health benefits associated with the consumption of prebiotic short-chain fructooligosaccharides (sc-FOS) and inulooligosaccharides (IOS), there is increased interest in the use of these compounds in food products. We have developed a new biocatalyst for the production of FOS and IOS by inulin hydrolysis. Endoinulinase from Aspergillus niger Inulinase ® Novozym 960 (Novozymes) was immobilised on polyhydroxybutyrate (PHB) nanofibres and microfibres by hydrophobic interactions. The PHB fibres were prepared by centrifugal spinning. FOS and IOS profiles were determined by ion-exchange chromatography with the Rezex RSO-Oligosaccharide column. The biocatalyst had very good activity and stability after repeated applications. It can be used in biocatalytic membrane reactors for the production of prebiotic oligosaccharides.

Response Surface Methodology-Based optimization of Inulinase Production from New Bacillus Isolates

“…For this, the effect of fructose, glucose, maltose, sucrose, lactose, onion peel, wheat bran, oat bran concentrations as carbon sources on enzyme production were evaluated, ranging from low to high. Concentrations of 0.1% and 1% levels Fermentation parameters including incubation period (1-4 days), incubation temperature (25-45 °C), and initial pH (5)(6)(7)(8) were also tested at 2 levels as high and low. For all tests, inulinase activity was taken as a response.…”

“…The type of carbon source used in the medium affects growth, sporulation, and cell wall structure in microorganisms, which in turn can affect the secretion of the enzyme [1,6]. Inulinases have different catalytic properties depending on the microbial origin such as molecular mass, optimum pH, optimum temperature, thermal and pH stabilities [7].…”

An enzymatic system for decolorization of wastewater dyes using immobilized CueO laccase‐like multicopper oxidase on poly‐3‐hydroxybutyrate

“…We have chosen polyhydroxybutyrate (PHB) as support, since it is the most commercially successful PHA and is present in a variety of manufactured products thanks to its versatility and cost-effectiveness (Yu, 2014). Moreover, PHB has been the subject of several protein immobilization studies by a variety of procedures (Backstrom et al, 2007;Deepak et al, 2009;Yang et al, 2015;Beran et al, 2016;Rehm et al, 2017). Decolorization was tested with the broad substrate range, bacterial laccase-like multicopper oxidase CueO, an enzyme that is involved in the copper homeostasis in E. coli (Grass and Rensing, 2001;Singh et al, 2004).…”

Produção de biocatalisador através da técnica de adsorção física a partir da lipase de Burkholderia cepacia e o estudo da influência de aditivos no processo de imobilização

“…As técnicas mais comuns são: aprisionamento em redes poliméricas/ encapsulação, reticulação e adsorção física. A técnica utilizada varia de acordo com a enzima, dependendo da escolha na imobilização pode ocasionar mudança da estrutura da lipase devido as fortes interações ocorridas com o suporte, impulsionando o movimento da parte móvel localizada próximo ao sítio ativo chamada de tampa protetora ou lid, sua movimentação pode levar a inativação da enzima por cobrir o sítio ativo, impedindo a formação do bioproduto (Beran et al, 2016).…”