Immobilization of β-galactosidase on Novel Polymers Having Schiff Bases

Figures & data

Figure 1. Mechanism of (A) for (APS-2PIn-Sch), (B) for (APS-2PIn-Sch-Ni) and (C) for Ni(II)-Aldehyde complexes.

Table 1. Analytical and physical data of the studied polymer.

Abbreviation (Mw)	mol/g N loading	mol/g Ni loading	Color
(APS)	0.53	–	deep cream
(APS-2PIn-Ald)	1.03	–	light yellow
(APS-2PIn-Ald-Ni)	1.01	0.51	light green

Table 2. Ir bands (cm⁻¹), electronic spectral (nm) (ε_max, mol⁻¹cm⁻¹L), and thermal analysis data of the studied polymers.

				Thermally Decomposed
Compound	υ(CH2)as,s υ(CH)as,s	υ(MN) υ(CH = N)	λmax (Absorbans)	Ti	T½	Tmax	Tf	Residue at 600°C (wt%)
(APS)	2963, 2872		272 (1.02), 306 (2.25)	368	409	413	432	2.2
(APS–2PIn-Sch)	2963, 2872	–	254 (2.9), 272 (0.54)	391	411	414	430	2.1
	3004, 3110	1587	302 (1.04)	389	405	407	423	2.1
(APS–2PIn-Sch–Ni)	2964, 2871	410	312 (4.00), 320 (12)
	3005, 3111	1571	416 (32), 620 (0.268) 693 (0.201)

T_i: Temperature of initial degradation. T_max: Temperature of maximum degradation.

T_f: Temperature of finally degradation. T_½: Temperature of half degradation.

Figure 2. Sem migrograph of studied polymers.

Figure 3. Effect of pH (A) and temperature (B) on enzyme activity and effect of reuse of immobilized β-galactosidase (C).

Figure 4. Suggested mechanism of enzyme immobilization on polymer support.

Figure 5. Lineweaver-Burk plots for free and immobilized β-galactosidase.