作者: P.R. Heinen , M.G. Pereira , C.G.V. Rechia , P.Z. Almeida , L.M.O. Monteiro
DOI: 10.1016/J.PROCBIO.2016.11.021
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摘要: Abstract An endo-xylanase produced by Aspergillus tamarii Kita was purified using the support CM-cellulose. The enzyme immobilized on CM-cellulose, glyoxyl-agarose and CNBr-agarose, but best considered since its derivative had more stability than CNBr-agarose (control) in broad range of temperature. derivatives an important hyperactivation (2.4-fold) CM-cellulose (5.1-fold). immobilization improved physicochemical parameters, increased optimum temperature 5 degrees, which changed from 60 °C control to 65 °C after multipoint covalent immobilization. Thermostability showed half-life (t0.5) values 96 60 min at 70 80 °C, respectively. Both apparent pH 5.5. Glyoxyl-agarose used consecutive cycles, maintaining 80% residual activity. be a very useful method for improving thermostability up 80 °C enabled successfully produce xylooligosaccharides (XOS) 2–5 degree polymerization (DP 2–5), especially xylotriose (39.7%) xylotetraose (29.4%), high temperatures. is potential resource numerous biotechnological processes, large scale production XOS could as prebiotic supplementation.