Grafted carrageenan: alginate gel beads for catalase enzyme covalent immobilization

被引:7
作者
Ali, Ali O. [1 ,4 ]
Abdalla, Mohga S. [2 ]
Shahein, Yasser E. [1 ]
Shokeer, Abeer [1 ]
Sharada, Hayat M. [2 ]
Ali, Korany A. [3 ,4 ]
机构
[1] Natl Res Ctr, Genet Engn & Biotechnol Div, Dept Mol Biol, El Behouth St, Cairo 12622, Egypt
[2] Helwan Univ, Dept Chem, Fac Sci, Helwan 11795, Egypt
[3] Natl Res Ctr, Dept Appl Organ Chem, El Behouth St, Cairo 12622, Egypt
[4] Natl Res Ctr, Adv Matrial & Nanotechnol Grp, Ctr Excellence Adv Sci, Cairo 12622, Egypt
关键词
Biotechnology; Biopolymers; Enzymes; Immobilized catalase and grafted gel beads; ENCAPSULATION; DISKS;
D O I
10.1007/s13205-021-02875-9
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A new matrix formulation was devised for catalase immobilization. Carrageenan-alginate beads different ratios were developed and soaked into different ratios of CaCl2-KCl as a hardening solution. The best formulation for loading capacity was selected, treated with polyethylene imine followed by glutaraldehyde and further studied. The best concentration of catalase for immobilization was 300U/ml and the best loading time was 6 h. The catalytic properties increased after immobilization and the immobilized catalase achieved optimum activity at a temperature range of 30-50 degrees C that was compared to the optimum activity of free catalase which occurred at 40 degrees C. Higher catalytic activity of immobilized catalase occurred at alkaline pHs than the free one which achieved optimum catalytic activity at neutral pH. A comparison between the kinetic parameters of immobilized and free catalase showed variation. The K-M and Vmax of the immobilized catalase were 2.4 fold and six times higher than those of free catalase. The results of the study indicate that the formulated matrix can be used as a good matrix for catalase enzyme in various industrial applications.
引用
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页数:7
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