Diverse Enzymes With Industrial Applications in Four Thraustochytrid Genera.

Autor: Lin HC; Department of Marine Biotechnology and Resources, National Sun Yat-sen University, Kaohsiung, Taiwan.; Doctoral Degree Program in Marine Biotechnology, National Sun Yat-sen University, Kaohsiung, Taiwan., Li WH; Department of Marine Biotechnology and Resources, National Sun Yat-sen University, Kaohsiung, Taiwan., Chen CC; Department of Marine Biotechnology and Resources, National Sun Yat-sen University, Kaohsiung, Taiwan., Cheng TH; Department of Marine Biotechnology and Resources, National Sun Yat-sen University, Kaohsiung, Taiwan., Lan YH; Department of Marine Biotechnology and Resources, National Sun Yat-sen University, Kaohsiung, Taiwan., Huang MD; Department of Biological Sciences, National Sun Yat-sen University, Kaohsiung, Taiwan., Chen WM; Department of Seafood Science, National Kaohsiung University of Science and Technology, Kaohsiung, Taiwan., Chang JS; Department of Chemical and Materials Engineering, College of Engineering, Tunghai University, Taichung, Taiwan.; Research Center for Smart Sustainable Circular Economy, Tunghai University, Taichung, Taiwan.; Department of Chemical Engineering, National Cheng Kung University, Tainan, Taiwan., Chang HY; Department of Marine Biotechnology and Resources, National Sun Yat-sen University, Kaohsiung, Taiwan.; Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan.
Jazyk: angličtina
Zdroj: Frontiers in microbiology [Front Microbiol] 2020 Oct 20; Vol. 11, pp. 573907. Date of Electronic Publication: 2020 Oct 20 (Print Publication: 2020).
DOI: 10.3389/fmicb.2020.573907
Abstrakt: Thraustochytrids are heterotrophic fungus-like protists that can dissolve organic matters with enzymes. Four strains, AP45, ASP1, ASP2, and ASP4, were isolated from the coastal water of Taiwan, and respectively identified as Aurantiochytrium sp., Schizochytrium sp., Parietichytrium sp., and Botryochytrium sp. based on 18S rRNA sequences. Transcriptome datasets of these four strains at days 3-5 were generated using Next Generation Sequencing technology, and screened for enzymes with potential industrial applications. Functional annotations based on KEGG database suggest that many unigenes of all four strains were related to the pathways of industrial enzymes. Most of all four strains contained homologous genes for 15 out of the 17 targeted enzymes, and had extra- and/or intra-cellular enzymatic activities, including urease, asparaginase, lipase, glucosidase, alkaline phosphatase and protease. Complete amino sequences of the first-time identified L-asparaginase and phytase in thraustochytrids were retrieved, and respectively categorized to the Type I and BPPhy families based on phylogenetic relationships, protein structural modeling and active sites. Milligram quantities of highly purified, soluble protein of urease and L-asparaginase were successfully harvested and analyzed for recombinant enzymatic activities. These analytical results highlight the diverse enzymes for wide-range applications in thraustochytrids.
(Copyright © 2020 Lin, Li, Chen, Cheng, Lan, Huang, Chen, Chang and Chang.)
Databáze: MEDLINE