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首页> 美国卫生研究院文献>Biochemical Journal >Cellulose hydrolysis by the cellulases from Trichoderma reesei: adsorptions of two cellobiohydrolases two endocellulases and their core proteins on filter paper and their relation to hydrolysis.
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Cellulose hydrolysis by the cellulases from Trichoderma reesei: adsorptions of two cellobiohydrolases two endocellulases and their core proteins on filter paper and their relation to hydrolysis.

机译：里氏木霉纤维素酶的纤维素水解作用：两种纤维二糖水解酶两种内切纤维素酶及其核心蛋白在滤纸上的吸附及其与水解的关系。

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摘要

Separate binding of several purified cellulolytic components of Trichoderma reesei on to filter paper was studied and concomitant hydrolysis rates evaluated. Enhancement of mass transfer from the bulk liquid to the solid substrate by agitation has two different effects on adsorption depending on the type of enzyme: (i) the fraction of cellobiohydrolase II (CBH II) and endoglucanase III (EG III) bound at equilibrium is increased, whereas (ii) the rate but not the extent of cellobiohydrolase I (CBH I) and endoglucanase I (EG I) adsorption is affected. The adsorption of CBH I core, a component lacking the cellulose-binding domain (CBD), is, however, not significantly influenced by mass transfer. The CBH I interdomain peptide (present in CBH I core b) does not participate in adsorption but enhances stability. The adsorption of CBH I core proteins is a fully reversible process whereas that of the intact CBH I is not. Thus, the interaction of the CBD with filter paper apparently accounts for the mass-transfer-limited binding rate and also for the irreversible adsorption of intact CBH I. Adsorption isotherms at 50 degrees C indicate very similar relative association constants for the intact cellulases (0.24-0.30 l/g of cellulose), but drastically reduced values for CBH I core proteins (0.03 l/g of cellulose). The specific activities of adsorbed CBH I and of its core proteins are identical and a linear relationship between adsorption and rates of hydrolysis is found only for these enzymes. Thus, non-productive binding on to cellulose seems evident in the case of CBH II and EG III but not CBH I.
机译：研究了几种纯化的里氏木霉纤维素分解成分在滤纸上的独立结合，并评估了相应的水解速率。取决于酶的类型，通过搅动增强从大块液体到固体基质的传质对吸附有两种不同的影响：（i）平衡结合的纤维二糖水解酶II（CBH II）和内切葡聚糖酶III（EG III）的比例为：增加（ii）纤维二糖水解酶I（CBH I）和内切葡聚糖酶I（EG I）的吸附速率但不受影响。然而，CBH I核心（一种缺乏纤维素结合域（CBD）的成分）的吸附不受传质的影响。 CBH I域间肽（存在于CBH I核心b中）不参与吸附，但可以提高稳定性。 CBH I核心蛋白的吸附是一个完全可逆的过程，而完整CBH I的吸附则不是。因此，CBD与滤纸的相互作用显然是由于传质受限的结合速率，也是完整CBH I不可逆吸附的原因.50摄氏度下的吸附等温线表明，完整纤维素酶的相对缔合常数非常相似（0.24 -0.30 l / g纤维素），但CBH I核心蛋白的值（0.03 l / g纤维素）大大降低。吸附的CBH I及其核心蛋白的比活性相同，仅对这些酶而言，吸附和水解速率之间存在线性关系。因此，在CBH II和EG III的情况下，与纤维素的非生产性结合似乎很明显，但在CBH I的情况下却没有。

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