ArticleWorld journal of microbiology & biotechnology2019
High-level secretive expression of a novel achieved Talaromyces cellulolyticus endo-polygalacturonase in Pichia pastoris by improving gene dosage for hydrolysis of natural pectin.
Article in World journal of microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 9 citations in OpenAlex.
- Oral Immunization with Yeast-Surface Display of SARS-CoV-2 Antigens inInfectious disease reports · 2025Article
- Improving the specific activity and stability of alkaline pectinase PEL3 through SpyTag/SpyCatcher cyclization.Biotechnology letters · 2023Article
- Heterologous Expression and Characterization of a Novel Exo-Polygalacturonase fromJournal of microbiology and biotechnology · 2023Article
- Production of Industrial Enzymes via Pichia pastoris as a Cell Factory in Bioreactor: Current Status and Future Aspects.The protein journal · 2021Review
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Pectin is a type of complex hydrophilic polysaccharide widely distributed in plant resources. Thermal stable pectinase has its advantage in bioapplication in the fields of food processing, brewing, and papermaking, etc. In this study, we enzymatically characterized a putative endo-polygalacturonase TcPG from a Talaromyces cellulolyticus, realized its high-level expression in Pichia pastoris by in vitro constructing of a series of multi-copy expression cassettes and real time quantitative PCR screening. The secretive expression level of TcPG was nonlinear correlated to the gene dosage. Recombinants with five-copy TcPG gene in the host genome showed the highest expression. After cultivation in a bioreactor for about 96 h, the enzyme activity reached 7124.8 U/mL culture. TcPG has its optimal temperature of 70 °C. Under the optimized parameters, the pectin could be efficiently hydrolyzed into oligosaccharides.
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