High level expression of Saccharomyces cerevisiae chitinase (ScCTS1) in Pichia pastoris for degrading chitin

Authors

  • Zhao Youxi 1. The Key Lab of Industrial Biotechnology, the Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China; 2. Beijing Key Laboratory of Biomass Waste Resource Utilization, Biochemical Engineering College, Beijing Union University, Beijing 100023, China;
  • Jiang Huihui 1. The Key Lab of Industrial Biotechnology, the Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China;
  • Rao Zhiming 1. The Key Lab of Industrial Biotechnology, the Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China;
  • Ji Yizhi 2. Beijing Key Laboratory of Biomass Waste Resource Utilization, Biochemical Engineering College, Beijing Union University, Beijing 100023, China;
  • Cheng Yanling 2. Beijing Key Laboratory of Biomass Waste Resource Utilization, Biochemical Engineering College, Beijing Union University, Beijing 100023, China;
  • Ma Yanhe 3. State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China

DOI:

https://doi.org/10.25165/ijabe.v8i5.2071

Keywords:

chitinases, heterologous expression, Saccharomyces cerevisiae, pichia pastoris, biotechnology

Abstract

Chitin is the second most abundant renewable biopolymer in the world. Chitinases play important roles in the degradation of chitin. Chitinases are produced by different organisms for different purposes, which are widely expressed in the three domains of life, ranging from archaea, bacteria, to fungi, yeasts, plants, insects, and even vertebrates. But there are few reports about Saccharomyces cerevisiae chitinase (ScCTS1). The aim of this study was to realize the high level expression of ScCTS1. The ScCTS1 was cloned into the expression vector pPIC9K. The recombinant plasmid was linearized and transformed into competent Pichia pastoris GS115. After screening by G418 plate, the fermentation conditions were optimized. Ultimately, under the optimal fermentation conditions, ScCTS1 enzymatic activity reached up to 94.6 U/mL. This paper presents the first report on the heterologous expression of a full-length ScCTS1 with considerably high activity. The work will not only make a great stride towards its potential applications in biotechnology, but also facilitate elucidating the precise mechanism of yeast cell division. Keywords: chitinases, heterologous expression, Saccharomyces cerevisiae, pichia pastoris, biotechnology DOI: 10.3965/j.ijabe.20150805.2071 Citation: Zhao Y X, Jiang H H, Rao Z M, Ji Y Z, Cheng Y L, Ma Y H. High level expression of Saccharomyces cerevisiae chitinase (ScCTS1) in Pichia pastoris for degrading chitin. Int J Agric & Biol Eng, 2015; 8(5): 142－150.

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Published

2015-10-31

How to Cite

Youxi, Z., Huihui, J., Zhiming, R., Yizhi, J., Yanling, C., & Yanhe, M. (2015). High level expression of Saccharomyces cerevisiae chitinase (ScCTS1) in Pichia pastoris for degrading chitin. International Journal of Agricultural and Biological Engineering, 8(5), 142–150. https://doi.org/10.25165/ijabe.v8i5.2071

Issue

Vol. 8 No. 5 (2015): IJABE

Section

Agro-product and Food Processing Systems

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