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  • what is c2 australia Conclusion By generating high quality h

    2021-11-29

    Conclusion By generating high-quality hypocotyl transcriptomes of a jute hypocotyl-defect mutant and its wild-type comprising the largest number of annotated unigenes (39,076), we identified a complete array of structurally and functionally diverse β-galactosidases. Our proposed domain-centric classification suggests the evolution of GH-35 family β-galactosidases through gene duplication and domain integration. We also report, for the first time, a transcriptionally active bacterial GH-2 family β-galactosidase in jute and analyzed its evolutionary history across living organisms. Finally, we provided compelling evidences for a crucial role of β-galactosidase in jute hypocotyl development. Our results provide the first clue as to how β-galactosidase influences hypocotyl development in a fast growing species.
    Experimental
    Availability of data and materials
    Declaration of interest
    Acknowledgements This work was supported by the Indian Council of Agricultural Research under the ICAR-Central Research Institute for Jute and Allied Fibres project JBT 4.1 and ICAR-NPTC sub-project 3070. We also acknowledge with thanks the Xcelris Labs Limited, Ahmedabad for Illumina paired-end sequencing, raw data processing and qRT-PCR. Valuable comments and suggestions on the manuscript from the Editor and the anonymous reviewers are gratefully acknowledged.
    Introduction α-Galactosidase (EC3.2.1.22) is an exo-glycoside hydrolase that catalyzes the hydrolysis of α-1,6-linked terminal galactose residues from different galactooligosaccharide substrates, such as raffinose and stachyose. α-Galactosidase can be used in a broad range of industrial fields [1]. In the feed industry, α-galactosidase plays a role in the hydrolysis of antinutritional what is c2 australia in soybean meal feeds, improving their nutritional utilization [2]. In the pulp and paper industry, α-galactosidase can improve the bleaching effect of endo-1,4-mannanase on softwood kraft pulp [3]. Furthermore, α-galactosidase can even be used for blood group transformation [4] and Fabry's treatment [5]. In the field of enzyme engineering, the efficient secretion of enzymes into the extracellular space has major advantages for downstream bioengineering processes and bioapplications. It simplified and facilitated the isolation, purification, and the formulation processes of enzymes and made them economically competitive for industrial applications [6]. Increasing the gene dosage in the host genome is generally regarded as an efficient method to improve the secretive expression levels of the enzymes [7,8]. Gene dosage, i.e., the RNA abundance at the transcriptional level, was a limiting element for high level expression of the targeted gene. In Pichia pastoris, a commonly used method to obtain high-level expression recombinants was to randomly select Pichia recombinants transformed with the heterogeneous genes under pressure from high concentrations of antibiotics, as the foreign gene can insert into the Pichia genome with multiple copies [6]. Artificially constructing multicopy expression cassettes and then transforming them into the host cells was proved to be an efficient measure to obtain Pichia recombinants with multiple insertions of a foreign gene. This strategy has been gradually used to improve the expression levels of exogenous proteins in P. pastoris [7,8]. However, high-level expression at the transcriptional or translational level of genes does not always lead to the efficient secretion of the protein. The abundantly expressed exogenous protein might not be secreted into the extracellular space due to issues with posttranslational processing in the endoplasmic reticulum of cells [9]. To counteract the accumulation of misfolded proteins, cells can initiate the unfolded protein response pathway in the endoplasmic reticulum [10]. Factors such as stress response protein (HAC1), protein disulfide isomerase (PDI and EroI), and molecular chaperones (Hsp40) are activated to promote the formation of disulfide bonds to let protein correctly folded or triggered the degradation of unfolded proteins for the recycling of amino acid materials. Thus, in bioengineering fields, improving the expression levels of endoplasmic reticulum secretion-associated factors (ERSAs) might increase the secretion of the protein into the extracellular space [[11], [12], [13]].