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The pH-activity profile of free LiP displayed optimal activity at pH 6 whereas, immobilization hyper-activated the LiP and slightly shifted pH optima towards more acidic pH range.
The pH optima for both crude and purified tannase were pH 5. The enzymes were found active in the pH range of 3 8 with an optimal activity at pH 5 (22.27 U/mg).
Amy13A is highly thermoactive, exhibiting optimal activity at 80 °C, and it is also highly salt-tolerant, being active in 25 % (w/v) NaCl.
CO hydrogenation rate increased with H2 composition reaching optimal activity at yH2 between 0.67 and 0.75.
Free α-galactosidase showed optimal activity at pH 5.8, immobilized α-galactosidase showed at 5.2 5.6.
At 37 °C it shows optimal activity at pH 5.5 6.
The purified enzyme had an optimal activity at pH 3.0 4.0 and 50 66 °C.
The purified enzyme showed optimal activity at 85 °C and pH 6.5.
Biochemical studies with peptide substrates indicate that cathepsins have optimal activity at acidic pH and highly attenuated activity at neutral pH.
The enzyme hydrolyzed barley β-glucan, carboxymethyl cellulose, lichenan, wheat arabinoxylan and birchwood xylan showing optimal activity at pH 8 and 65 °C.
The enzyme exhibited an optimal activity at pH 5.0 and 40 °C and retained over 20% of maximal activity over the temperature range 0 20 °C.
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