Effect of chitosan molecular weight on the formation of chitosan–pullulanase soluble complexes and their application in the immobilization of pullulanase onto Fe3O4–κ-carrageenan nanoparticles. (1st July 2016)

• Record Type: Journal Article
• Authors: Long, Jie; Xu, Enbo; Li, Xingfei; Wu, Zhengzong; Wang, Fang; Xu, Xueming; Jin, Zhengyu; Jiao, Aiquan; Zhan, Xiaobei
• Is Part Of: Food chemistry. Volume 202(2016)
• Page Start: 49
• Page End: 58
• Publication Date: 2016-07-01
• Subjects: Chitosan -- Molecular weight -- Pullulanase -- Complex -- Fe3O4–κ-carrageenan nanoparticles; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2016.01.119
• Languages: English
• ISSNs: 0308-8146

Abstract

Graphical abstract: Highlights: Complexation of chitosan and pullulanase was affected by chitosan molecular weight. Pullulanase was immobilized onto Fe3 O4 –κ-carrageenan nanoparticles by complexation. Interrelationship exists between chitosan Mw and binding characteristic. The high binding affinity induces more alterations of protein secondary structure. Changes in secondary structures impact enzymatic properties of immobilized enzyme. Abstract: The interactions between pullulanase and chitosans of different molecular weights (Mw) were comprehensively studied, and their applications in pullulanase immobilization onto Fe3 O4 –κ-carrageenan nanoparticles upon chitosan–pullulanase complexation were also evaluated. Chitosan (CS) complexation with pullulanase was found to be dependent on pH and chitosan Mw. The critical pH of structure-forming events during complexation shifted significantly ( p < 0.05) to a lower pH with a low Mw chitosan (50 kDa) compared to other chitosan types. Binding constants for the chitosan–pullulanase interaction increased in the following order: CS-500 < CS-400 < CS-50 < CS-200. The binding induced alterations in the protein secondary structure, which may affect the enzymatic properties of immobilized pullulanase. Pullulanase immobilized upon CS-50 complexation exhibited the most desirable enzymatic properties. These results indicated that the complexation behavior was mainly dependent on chitosan Mw. This study presents a technique for the production of immobilized pullulanase upon complexation that exhibits potential for applications in continuous syrup production.