Ugarova N N, Kershengol'ts B M, Artamonov I D, Berezin I V
Biokhimiia. 1976 Sep;41(9):1662-70.
Effect of polyacrylamide (PAA) gel on properties of horseradish peroxidase, immobilized by means of the incorporation into PAA gel is studied. Catalytic properties of immobilized enzyme are studied. Km value and pH-dependency of the enzyme activity are found to be close to those of soluble enzyme, kcat value is 3 times lower at pH 7.0. PH-stability of immobilized peroxidase at 20 degrees C and thermostability of soluble and immobilized peroxidases at pH 7.0 within the temperature range from 20 to 81 degrees C are studied. The stability of peroxidase in PAA gel is found to decrease (in 3 times at 20 degrees C, and in 17 times at 56 degrees C). A mechanism of the effect of PAA gel on catalytic properties and stability of peroxidase is discussed.
研究了通过掺入聚丙烯酰胺（PAA）凝胶固定辣根过氧化物酶时，PAA凝胶对其性质的影响。对固定化酶的催化性质进行了研究。发现固定化酶的Km值和酶活性的pH依赖性与可溶性酶相近，在pH 7.0时kcat值低3倍。研究了固定化过氧化物酶在20℃下的pH稳定性以及可溶性和固定化过氧化物酶在pH 7.0、20至81℃温度范围内的热稳定性。发现过氧化物酶在PAA凝胶中的稳定性降低（在20℃时降低3倍，在56℃时降低17倍）。讨论了PAA凝胶对过氧化物酶催化性质和稳定性影响的机制。
