Immobilized endo-xylanase of Aspergillus tamarii Kita: an interesting biological tool for production of xylooligosaccharides at high temperatures. (February 2017)

• Record Type: Journal Article
• Authors: Heinen, P.R.; Pereira, M.G.; Rechia, C.G.V.; Almeida, P.Z.; Monteiro, L.M.O.; Pasin, T.M.; Messias, J.M.; Cereia, M.; Kadowaki, M.K.; Jorge, J.A.; Polizeli, M.L.T.M.
• Is Part Of: Process biochemistry. Volume 53(2017)
• Page Start: 145
• Page End: 152
• Publication Date: 2017-02
• Subjects: Endo-xylanase -- Immobilization -- Thermostability -- Xylooligosaccharides -- CM-cellulose support -- Glyoxyl-agarose support; Biochemical engineering -- Periodicals; Biotechnology -- Periodicals; Biochemistry -- periodicals; Biotechnology -- periodicals; Chemical Engineering -- periodicals; Génie biochimique -- Périodiques; Biotechnologie -- Périodiques; Biochemical engineering; Biotechnology; Periodicals; 660.63
• DOI: 10.1016/j.procbio.2016.11.021
• Languages: English
• ISSNs: 1359-5113

Abstract

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