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重组双功能融合蛋白的形成:将两种酶的活性结合在单个蛋白中的一种新方法。

Formation of recombinant bifunctional fusion protein: A newer approach to combine the activities of two enzymes in a single protein.

机构信息

Department of Plant Molecular Biology and Biotechnology, ASPEE College of Horticulture and Forestry, Navsari Agricultural University, Navsari, Gujarat, India.

Department of Microbiology, PSGVP Mandal's S. I. Patil Arts, G B Patel Science & STKVS Commerce College, Shahada, Maharashtra, India.

出版信息

PLoS One. 2022 Apr 1;17(4):e0265969. doi: 10.1371/journal.pone.0265969. eCollection 2022.

Abstract

The tissue of insects, pests, and fungi has a chitin layer followed by protein in the cell membrane. The complete biodegradation of chitin and protein-present in the waste requires the action of two enzymes, namely chitinase, and protease. Combining chitinase and protease in a single protein/enzyme will serve as a bifunctional enzyme that can efficiently degrade the chitin and protein-rich biomass. The present study was aimed to fuse these two enzymes to produce a single protein and study the kinetics of the recombinant fusion protein. A chitinase and alkaline protease genes were isolated, cloned, and expressed successfully as a fusion product in heterologous host Escherichia coli. The two native genes were successfully fused in E.coli by using flexible glycine-serine (G4S)2 linker (GGGGS, GS linker). The recombinant fusion protein in E.coli showed hydrolyzed chitin and protein on chitin and bovine serum albumin agar plates confirming the successful cloning and expression of chitinase and protease enzymes in a single fusion protein. The common pUC18-T7 mini vector with the ompA signal sequence helps the extracellular expression of fusion protein efficiently. The native gel electrophoresis revealed a molecular mass of purified protein as 92.0 kDa. The fusion protein's maximal chitinase and protease activity occurred at pH 5.0 and 8.0 and 30 0C, respectively resembling the individual enzymes'. In the kinetic studies of the fusion protein, it was observed that the presence of metal ions such as Cu2+, Na2+, and Ca2+; significantly enhanced the enzyme activities while organic solvents oxidants and chemicals have drastically affected the activities of both the enzymes in the fusion protein. No such fusion protein has been produced in a heterologous host yet. The reports on fusion protein with biomass-degrading capacity are also scarce. This is probably the first report of a bifunctional chitinase/protease expressed in E. coli.

摘要

昆虫、害虫和真菌的组织具有几丁质层,随后是细胞膜中的蛋白质。要完全生物降解废物中的几丁质和蛋白质,需要两种酶的作用,即几丁质酶和蛋白酶。将几丁质酶和蛋白酶结合在单一蛋白质/酶中,将作为一种双功能酶,可以有效地降解富含几丁质和蛋白质的生物质。本研究旨在融合这两种酶以产生一种单一蛋白质,并研究重组融合蛋白的动力学。成功地从昆虫中分离、克隆和表达了几丁质酶和碱性蛋白酶基因,并作为异源宿主大肠杆菌中的融合产物表达。通过使用柔性甘氨酸-丝氨酸(G4S)2 接头(GGGGS、GS 接头),成功地将两个天然基因融合到大肠杆菌中。重组融合蛋白在大肠杆菌中显示出对几丁质和牛血清白蛋白琼脂平板的水解作用,证实了几丁质酶和蛋白酶在单一融合蛋白中的成功克隆和表达。带有 ompA 信号序列的常见 pUC18-T7 微型载体有助于融合蛋白的有效细胞外表达。天然凝胶电泳显示纯化蛋白的分子量为 92.0 kDa。融合蛋白的最大几丁质酶和蛋白酶活性分别在 pH 5.0 和 8.0 和 30°C 时发生,类似于各自的酶。在融合蛋白的动力学研究中,观察到金属离子如 Cu2+、Na2+和 Ca2+的存在显著增强了酶活性,而有机溶剂氧化剂和化学品则严重影响了融合蛋白中两种酶的活性。尚未在异源宿主中产生这种融合蛋白。关于具有生物质降解能力的融合蛋白的报告也很少。这可能是首次在大肠杆菌中表达的双功能几丁质酶/蛋白酶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dacc/8975109/8eae77f8e1e4/pone.0265969.g001.jpg

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