中文摘要：

如何提高酶蛋白的热稳定性是分子生物学、微生物学、生化工程学等学科长期所关注的重要研究课题之一．本文研究了多种添加剂对绿色木霉纤维素酶热稳定性的影响．在60℃的溶液中，多元醇（乙二醇、甘油、赤藓糖醇、木糖醇和山梨糖醇）能提高该酶的热稳定性，随着浓度的增加，赤藓糖醇、木糖醇和山梨糖醇促进酶的热稳定性呈线性增高；适当的多元醇分子长度对该酶的热稳定性有最优的保护效应；不同浓度和不同分子量的聚乙二醇对该酶的热稳定性具有明显的影响；在无机盐中，单价金属阳离子比二价金属阳离子更能显著地提高该酶的热稳定性；酶液溶剂的改变直接影响着该酶的热稳定性，该酶在D2O溶液中比在水溶液中稳定，其酶活半衰期延长了2．6倍．研究表明，热环境使酶蛋白分子的螺旋结构发生变化而失活，但某些溶质和溶剂的存在可能通过作用于蛋白质分子的三维结构而影响该酶的热稳定性．图7参15

英文摘要：

In order to establish a more general mechanism of enzyme stabilization, it is necessary to study the behavior of other types of enzymes in the presence of various additives. The effect of different additives （polyhydric alcohols, polyethylene glycol and salts） on the thermostability of Trichoderma viride cellulase at 60℃ was studied in aqueous medium. The results showed that the effect was stabilized in the presence of polyhydric alcohols （ethylene glycol, glycerol, erythritol, xylitol and sorbitol） and most of the polyethylene glycol. The effect of the monovalent ions on cellulase thermostability could be correlated to the lyotropic series of Hofmeister. The thermal denaturation of cellulase was performed in a 97% deuterium water medium. In this medium, the enzyme was more stable and its half life was 2.6-fold higher than that in normal water. Considering the results obtained with cellulase stability in the presence of polyhydrie alcohols, PEG, salts and D20, it is possible to propose a more general mechanism of enzyme stabilization. Fig 7, Ref 15