Immobilization of glutaminase enzyme from Hypocria jecorina on polyacrylic acid: preparation and biochemical characterization

Figures & data

Scheme 1. The hypothetical structure of ternary PAA-Cu²⁺–glutaminase enzyme from Hypocrea jecorina complex.

Table I. Immobilization of glutaminase enzyme from Hypocrea Jecorina.

	NH4^+ amount liberated from L-Glutaminase reaction (mg/mL) ± s*	L-Glutaminase activity (U/mL) ± s*	Protein amount (mg/mL) ± s*	Specific activity (U/mg protein) ± s*
Free enzyme	4.42 ± 0.5	13.75 ± 0.9	0.34 ± 0.8	40.32 ± 0.5
PAA-Cu ^2+-glutaminase triple complex	3.86 ± 0.4	8.65 ± 0.6	0.24 ± 0.4	36.45 ± 0.5

*s: Standard deviation. The data were calculated from the results obtained from triplicated experiments as mentioned section.

Figure 1. Effect of pH on free and immobilized L-glutaminase enzyme produced from Hypocrea jecorina.

Figure 2. Effect of temperature on free and immobilized L-glutaminase enzyme produced from Hypocrea jecorina.

Figure 3. Thermal stability of free L-glutaminase from Hypocrea Jecorina.

Figure 4. Thermal stability of immobilized L-glutaminase from Hypocrea Jecorina.

Table II. The kinetic properties of free and immobilized L-glutaminase from Hypocrea Jecorina.

Enzyme	Km (mM)	Vmax (U/L)
Free	0.49	13.86
İmmobilized	0.38	10.9

Figure 5. Storage stability of free and immobilized L-glutaminase from Hypocrea Jecorina at + 4°C.