Sud'ina E G, Samartsev M A, Golod M G, Dovbysh E F
Ukr Biokhim Zh (1978). 1979 Jul-Aug;51(4):404-8.
Immobilization of chlorophyllase was performed on aminohexadecyl sepharose, aminoundecyl sepharose and heptyl sepharose. The enzyme activity lowers considerably and is rather close for all carriers. Essential differences are manifested in stability of the preparation during storage. On aminohexadecyl sepharose, the most hydrophobic carrier, the activity of chlorophyllase is 1.4 times as low for a month, on aminoundecyl sepharose for the same period it is 2.1 times as low and on heptyl sepharose--4.8 times as low. The covalent binding of chlorophyllase with sepharose activated by bromo-cyanogen with the subsequent fixation of diethyl amine or dodecyl amine possessing different hydrophobic properties showed that diethyl amine favours to a greater extent manifestation of the chlorophyllase activity and stabilization of the enzyme in time than dodecylamine. The data obtained evidence for a considerable role of the enzyme sstate and its molecular environment in manifestation of its functional activity and in providing its stability.
叶绿素酶固定在氨基十六烷基琼脂糖、氨基十一烷基琼脂糖和庚基琼脂糖上。酶活性大幅降低，且在所有载体上相当接近。制剂在储存期间的稳定性表现出本质差异。在最疏水的载体氨基十六烷基琼脂糖上，一个月内叶绿素酶活性降低至原来的1.4倍，在氨基十一烷基琼脂糖上同一时期降低至2.1倍，在庚基琼脂糖上降低至4.8倍。叶绿素酶与经溴化氰活化的琼脂糖共价结合，随后固定具有不同疏水性质的二乙胺或十二胺，结果表明，与十二胺相比，二乙胺在更大程度上有利于叶绿素酶活性的表现以及酶随时间的稳定。所获得的数据证明了酶的状态及其分子环境在其功能活性表现和稳定性维持方面起着相当重要的作用。
