Nanoplatforms attached Schiff bases by condensation method; Investigation of glucose oxidase enzyme as biocatalysts

Figures & data

Figure 1. Synthesis route of nanoplatform supports for immobilization of GOx enzyme and SEM imaging.

Figure 2. Effect of pH and temperatur on enzyme activity of GOx-(PSA) and studied polymers.

Figure 3. Image of hydrogen and amid bond between GOx in the studied support polymers.

Figure 4. Kinetic parameters of free and immobilized GOx (♦:Free enzyme, ▲: (PSA-SalH), ■: (PSA-SalCH₃), x:(PSA)).

Table I. Elemental analysis and important physical properties of modified polymer.

Compound, Color, and *Mw	Chemical formula, (Mw, Mn), PDI, and C, H, and N; (% found/calc.)	IR spectra
		νNH2 ν>(OH),	νoverton νCH/CH2,	νCH = N υ(CH)bucking
(PSA) Crem, 848	[(C8H8)7(C6H4(CH2)2NH2)] (892, 586), 1.52 90.32/90.56, 7.79/7.78,1.88/1.65	3467 –	1940, 1870,1800 3013, 2920	– 554, 540
(PSA-SalH) Yellow, 836	[(C8H8)6(C12H10(CH2)2 NO)] (880, 807), 1.09 89.00/89.34,7.18/7.01,1.67/1.56	– 3432	1937, 1868, 1796 3013, 2920	1618 556, 543
(PSA-SalCH3) Yellow, 848	[(C8H8)6(C13H12(CH2)2 NO)] (898, 831), 1.08 89.15/88.56,7.55/7.23,1.65/1.34	– 3435	1941, 1870, 1803 3013, 2920	1622 556, 541

*Determined by elemental analyses.

Table II. SEM imaging (Mag 120 × and 500×) EDX spectra of studied polymer.

(PSA-Sch) n:	Imaging	Elemental composition (by EDX)%
		C	O
(PSA)		91.21	1.21
(PSA-SalH)		80.36	11.36
(PSA-SalCH3)		80.82	12.04

Table III. Kinetic parameters for free and immobilized GOxs.

Working Conditions	Immobilized GOx Free GOx Vmax (mM.min^− 1); Km (mM)
pH, t (°C)	(PSA)	(PSA-SalH)	(PSA-SalCH3)
4 80°C	1.641; 1.031	–	–	1.987; 0.819
6 40°C	–	–	0.706; 3.703	0.662; 0.909
6 70°C	–	–	2.216; 0.813	1.011; 0.826
7 80°C	1.266; 0.917	1.069; 0.549	–	1.799; 0.8440