Weiss B, Hui M, Lajtha A
Res Commun Chem Pathol Pharmacol. 1978 Nov;22(2):365-73.
Rat liver phenylalanine hydroxylase (PheH) was covalently coupled to AH-Sepharose 4B, CH-Sepharose 4B, alginic acid and polygalacturonic acid. The activities of the bound enzyme from the ethanol and ammonium sulfate fractions were studied under a variety of conditions. The ethanol enzyme coupled to AH-Sepharose 4B showed the best thermal stability from 20 degrees to 50 degrees after heating for 15 min. It retained more than 15% of its initial activity after storage at 25 degrees for 9 days. The covalently linked enzymes generally had a broader range of optimal activity from pH 5.8 to 7.5. The presence of a positive or negative microenvironment on the matrix had no effect on the activity of the enzyme coupled to AH- or CH-Sepharose 4B. The failure to obtain hydroxylase activity with enzyme linked to alginic acid or polygalacturonic acid was attributed to the acidic microenvironment of the matrices.
大鼠肝脏苯丙氨酸羟化酶（PheH）被共价偶联到琼脂糖凝胶4B、交联琼脂糖凝胶4B、海藻酸和聚半乳糖醛酸上。在多种条件下研究了来自乙醇和硫酸铵组分的结合酶的活性。与琼脂糖凝胶4B偶联的乙醇酶在20℃至50℃加热15分钟后表现出最佳热稳定性。在25℃储存9天后，它保留了超过15%的初始活性。共价连接的酶通常在pH 5.8至7.5范围内具有更宽的最佳活性范围。基质上正或负微环境的存在对与琼脂糖凝胶4B或交联琼脂糖凝胶4B偶联的酶的活性没有影响。未能获得与海藻酸或聚半乳糖醛酸连接的酶的羟化酶活性归因于基质的酸性微环境。
