ADSORPTION AND KINETIC-BEHAVIOR OF PURIFIED ENDOGLUCANASES AND EXOGLUCANASES FROM TRICHODERMA-VIRIDE
ADSORPTION AND KINETIC-BEHAVIOR OF PURIFIED ENDOGLUCANASES AND EXOGLUCANASES FROM TRICHODERMA-VIRIDE
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DOI：
10.1002/bit.260300215
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发表时间：
1987-08-05
影响因子：
3.8
通讯作者：
PILNIK, W
中科院分区：
文献类型：
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作者：
BELDMAN, G;VORAGEN, AGJ;PILNIK, W
研究了从绿色木霉商品化纤维素酶制剂中提纯的6种内切葡聚糖酶(Endo I、II、III、IV、V和VI；1，4-β-D-葡聚糖葡聚糖水解酶，EC 3.2.1.4)和2种外切葡聚糖酶(Exo II和III；1，4-β-D-葡聚糖纤维二糖水解酶，EC 3.2.1.92)在结晶纤维素上的吸附。Endo I、III和V在Avicel纤维上有较强的吸附，而Endo II、IV和VI的吸附较弱。此外，这两种外切葡聚糖酶还可以分为两种酶：一种是具有高吸附亲和力的酶(Exo III)，另一种是中等吸附的酶(Exo II)。吸附数据符合Langmuir型吸附等温式。然而，就稀释而言，吸附只是部分可逆的。以释放的水解物的多样性衡量，未发现吸附亲和力与纤维素水解的随机性程度之间的关系。动力学测试表明，只有部分被吸附的酶分子具有水解性。
Adsorption on crystalline cellulose of six endoglucanases (Endo I, II, III, IV, V and VI; 1,4-.beta.-D-glucan glucanohydrolase, EC 3.2.1.4) and two exoglucanases (Exo II and III; 1,4-.beta.-D-glucan cellobiohydrolase, EC 3.2.1.92), purified from a commercial cellulase preparation of Trichoderma viride origin, was studied. Endo I, III, and V adsorbed strongly on Avicel cellulose, while adsorption of Endo II, IV, and VI was much lower. Also, the two exoglucanases could be divided into one enzyme (Exo III) that had a high adsorption affinity and another enzyme (Exo II) that adsorbed only moderately. Adsorption data fitted the Langmuir-type adsorption isotherm. However, adsorption was only partially reversible with respect to dilution. No relation could be found between adsorption affinity and degree of randomness in cellulose hydrolysis, measured as the diversity of released hydrolytic products. Kinetic measurements indicated that only part of the adsorbed enzyme molecules are hydrolytically active.