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添加底物结合结构域可提高哈茨木霉几丁质酶的底物结合能力和比活性。

Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum.

作者信息

Limón M C, Margolles-Clark E, Benítez T, Penttilä M

机构信息

Departamento de Genética Facultad de Biologia, Universidad de Servilla, Apartado 1095, E-41080 Servilla, Spain.

出版信息

FEMS Microbiol Lett. 2001 Apr 20;198(1):57-63. doi: 10.1111/j.1574-6968.2001.tb10619.x.

Abstract

Chitinase Chit42 from Trichoderma harzianum CECT 2413 is considered to play an important role in the biocontrol activity of this fungus against plant pathogens. Chit42 lacks a chitin-binding domain (ChBD). We have produced hybrid chitinases with stronger chitin-binding capacity by fusing to Chit42 a ChBD from Nicotiana tabacum ChiA chitinase and the cellulose-binding domain from cellobiohydrolase II of Trichoderma reesei. The chimeric chitinases had similar activities towards soluble substrate but higher hydrolytic activity than the native chitinase on high molecular mass insoluble substrates such as ground chitin or chitin-rich fungal cell walls.

摘要

来自哈茨木霉CECT 2413的几丁质酶Chit42被认为在该真菌对植物病原体的生物防治活性中发挥重要作用。Chit42缺乏几丁质结合结构域(ChBD)。我们通过将烟草ChiA几丁质酶的ChBD和里氏木霉纤维二糖水解酶II的纤维素结合结构域与Chit42融合,产生了具有更强几丁质结合能力的杂合几丁质酶。嵌合几丁质酶对可溶性底物具有相似的活性,但在高分子量不溶性底物如磨碎的几丁质或富含几丁质的真菌细胞壁上,其水解活性高于天然几丁质酶。

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