[1]
|
Karbalaei, M., Rezaee, S.A. and Farsiani, H. (2020) Pichia pastoris: A Highly Successful Expression System for Opti-mal Synthesis of Heterologous Proteins. Journal of Cellular Physiology, 235, 5867-5881.
https://doi.org/10.1002/jcp.29583
|
[2]
|
Baghban, R., Farajnia, S., Rajabibazl, M., et al. (2019) Yeast Expression Systems: Overview and Recent Advances. Molecular Biotechnology, 61, 365-384. https://doi.org/10.1007/s12033-019-00164-8
|
[3]
|
De Schutter, K., Lin, Y.C., Tiels, P., et al. (2009) Genome Se-quence of the Recombinant Protein Production Host Pichia pastoris. Nature Biotechnology, 27, 561-566. https://doi.org/10.1038/nbt.1544
|
[4]
|
Puxbaum, V., Mattanovich, D. and Gasser, B. (2015) Quo Vadis? The Chal-lenges of Recombinant Protein Folding and Secretion in Pichia pastoris. Applied Microbiology and Biotechnology, 99, 2925-2938.
https://doi.org/10.1007/s00253-015-6470-z
|
[5]
|
Yu, P., Zhu, Q., Chen, K., et al. (2015) Improving the Secretory Production of the Heterologous Protein in Pichia pastoris by Focusing on Protein Folding. Applied Biochemistry and Bi-otechnology, 175, 535-548.
https://doi.org/10.1007/s12010-014-1292-5
|
[6]
|
Araki, K. and Nagata, K. (2012) Protein Folding and Quality Control in the ER. Cold Spring Harbor Perspectives in Biology, 4, a015438. https://doi.org/10.1101/cshperspect.a015438
|
[7]
|
Read, A. and Schröder, M. (2021) The Unfolded Protein Re-sponse: An Overview. Biology, 10, Article No. 384.
https://doi.org/10.3390/biology10050384
|
[8]
|
Snapp, E.L. (2012) Unfolded Protein Responses with or without Unfolded Proteins? Cells, 1, 926-950.
https://doi.org/10.3390/cells1040926
|
[9]
|
Damasceno, L.M., Pla, I., Chang, H.J., et al. (2004) An Optimized Fer-mentation Process for High-Level Production of a Single-Chain Fv Antibody Fragment in Pichia pastoris. Protein Ex-pression and Purification, 37, 18-26.
https://doi.org/10.1016/j.pep.2004.03.019
|
[10]
|
Elena, C., Ravasi, P., Cerminati, S., et al. (2016) Pichia pastoris Engineering for the Production of a Modified Phospholipase C. Process Biochemistry, 51, 1935-1944. https://doi.org/10.1016/j.procbio.2016.08.022
|
[11]
|
Yu, Y., Liu, Z., Chen, M., et al. (2020) Enhancing the Expres-sion of Recombinant κ-Carrageenase in Pichia pastoris Using Dual Promoters, Co-Expressing Chaperones and Tran-scription Factors. Biocatalysis and Biotransformation, 38, 104-113. https://doi.org/10.1080/10242422.2019.1655001
|
[12]
|
Shen, Q., Wu, M., Wang, H.B., et al. (2012) The Effect of Gene Copy Number and Co-Expression of Chaperone on Production of Albumin Fusion Proteins in Pichia pastoris. Ap-plied Microbiology and Biotechnology, 96, 763-772.
https://doi.org/10.1007/s00253-012-4337-0
|
[13]
|
Sha, C., Yu, X.W., Lin, N.X., et al. (2013) Enhancement of Li-pase r27RCL Production in Pichia pastoris by Regulating Gene Dosage and Co-Expression with Chaperone Protein Di-sulfide Isomerase. Enzyme and Microbial Technology, 53, 438-443. https://doi.org/10.1016/j.enzmictec.2013.09.009
|
[14]
|
Wang, L., Hu, T., Jiang, Z., et al. (2021) Efficient Production of a Novel Alkaline Cold-Active Phospholipase C from Aspergillus Oryzaeby Molecular Chaperon Co-Expression for Crude Oil Degumming. Food Chemistry, 350, Article ID: 129212. https://doi.org/10.1016/j.foodchem.2021.129212
|
[15]
|
He, H., Wu, S., Mei, M., et al. (2020) A Combinational Strategy for Effective Heterologous Production of Functional Human Lysozyme in Pichia Pastoris. Frontiers in Bioen-gineering and Biotechnology, 8, Article No. 118.
https://doi.org/10.3389/fbioe.2020.00118
|
[16]
|
Li, J., Cai, J., Ma, M., et al. (2021) Preparation of a Bombyx mori Acetylcholinesterase Enzyme Reagent through Chaperone Protein Disulfide Isomerase Co-Expression Strategy in Pichia pastoris for Detection of Pesticides. Enzyme and Microbial Technology, 144, Article ID: 109741. https://doi.org/10.1016/j.enzmictec.2020.109741
|
[17]
|
Navone, L., Vogl, T., Luangthongkam, P., et al. (2021) Di-sulfide Bond Engineering of AppA Phytase for Increased Thermostability Requires Co-Expression of Protein Disulfide Isomerase in Pichia pastoris. Biotechnology for Biofuels and Bioproducts, 14, 80. https://doi.org/10.1186/s13068-021-01936-8
|
[18]
|
Yang, J., Lu, Z., Chen, J., et al. (2016) Effect of Cooperation of Chaperones and Gene Dosage on the Expression of Porcine PGLYRP-1 in Pichia pastoris. Applied Microbiology and Biotechnology, 100, 5453-5465.
https://doi.org/10.1007/s00253-016-7372-4
|
[19]
|
Huang, J., Zhao, Q., Chen, L., et al. (2020) Improved Production of Recombinant Rhizomucor miehei Lipase by Coexpressing Protein Folding Chaperones in Pichia pastoris, Which Triggered ER Stress. Bioengineered, 11, 375-385.
https://doi.org/10.1080/21655979.2020.1738127
|
[20]
|
Guan, B., Chen, F., Su, S., et al. (2016) Effects of Co-Overexpression of Secretion Helper Factors on the Secretion of a HSA Fusion Protein (IL2-HSA) in Pichia pastoris. Yeast, 33, 587-600. https://doi.org/10.1002/yea.3183
|
[21]
|
Lan, D., Qu, M., Yang, B., et al. (2016) Enhancing Pro-duction of Lipase MAS1 from Marine Streptomyces sp. Strain in Pichia pastoris by Chaperones Co-Expression. Elec-tronic Journal of Biotechnology, 22, 62-67.
https://doi.org/10.1016/j.ejbt.2016.06.003
|
[22]
|
Duan, G., Ding, L., Wei, D., et al. (2019) Screening Endogenous Signal Peptides and Protein Folding Factors to Promote the Secretory Expression of Heterologous Proteins in Pichia pastoris. Journal of Biotechnology, 306, 193-202.
https://doi.org/10.1016/j.jbiotec.2019.06.297
|
[23]
|
Sallada, N.D., Harkins, L.E. and Berger, B.W. (2019) Effect of Gene Copy Number and Chaperone Coexpression on Recombinant Hydrophobin HFBI Biosurfactant Production in Pichia pastoris. Biotechnology and Bioengineering, 116, 2029-2040. https://doi.org/10.1002/bit.26982
|
[24]
|
Samuel, P., Prasanna Vadhana, A.K., Kamatchi, R., et al. (2013) Effect of Molecular Chaperones on the Expression of Candida antarctica Lipase B in Pichia pastoris. Microbiological Research, 168, 615-620.
https://doi.org/10.1016/j.micres.2013.06.007
|
[25]
|
Gasser, B., Sauer, M., Maurer, M., et al. (2007) Transcriptom-ics-Based Identification of Novel Factors Enhancing Heterologous Protein Secretion in Yeasts. Applied and Environ-mental Microbiology, 73, 6499-6507.
https://doi.org/10.1128/AEM.01196-07
|
[26]
|
Summpunn, P., Jomrit, J. and Panbangred, W. (2018) Improvement of Extracellular Bacterial Protein Production in Pichia pastoris by Co-Expression of Endoplasmic Reticulum Residing GroEL-GroES. Journal of Bioscience and Bioengineering, 125, 268-274. https://doi.org/10.1016/j.jbiosc.2017.09.007
|
[27]
|
Huo, X., Liu, Y., Wang, X., et al. (2007) Co-Expression of Hu-man Protein Disulfide Isomerase (hPDI) Enhances Secretion of Bovine Follicle-stimulating Hormone (bFSH) in Pichia pastoris. Protein Expression and Purification, 54, 234-239. https://doi.org/10.1016/j.pep.2007.03.016
|
[28]
|
Zhang, Z., Zhang, X., Hao, H., et al. (2020) Co-Expression of Pseudomonas alcaligenes Lipase and Its Specific Foldase in Pichia pastoris by a Dual Expression Cassette Strategy. Protein Expression and Purification, 175, Article ID: 105721. https://doi.org/10.1016/j.pep.2020.105721
|
[29]
|
Guerfal, M., Ryckaert, S., Jacobs, P.P., et al. (2010) The HAC1 Gene from Pichia pastoris: Characterization and Effect of Its Overexpression on the Production of Secreted, Surface Displayed and Membrane Proteins. Microbial Cell Factories, 9, Article No. 49. https://doi.org/10.1186/1475-2859-9-49
|
[30]
|
Fauzee, Y., Taniguchi, N., Ishiwata-Kimata, Y., et al. (2020) The Unfolded Protein Response in Pichia pastoris without External Stressing Stimuli. FEMS Yeast Research, 20, foaa053. https://doi.org/10.1093/femsyr/foaa053
|
[31]
|
Whyteside, G., Nor, R.M., Alcocer, M.J., et al. (2011) Activation of the Unfolded Protein Response in Pichia pastoris Requires Splicing of a HAC1 mRNA Intron and Retention of the C-Terminal Tail of Hac1p. FEBS Letters, 585, 1037-1041. https://doi.org/10.1016/j.febslet.2011.02.036
|
[32]
|
Han, M., Wang, W., Gong, X., et al. (2021) Increased Expression of Recombinant Chitosanase by Co-Expression of Hac1p in the Yeast Pichia pastoris. Protein and Peptide Letters, 28, 1434-1441.
https://doi.org/10.2174/0929866528666211105111155
|
[33]
|
Han, M., Wang, W., Zhou, J., et al. (2020) Activation of the Unfolded Protein Response via Co-Expression of the HAC1i Gene Enhances Expression of Recombinant Elastase in Pichia pastoris. Biotechnology and Bioprocess Engineering, 25, 302-307. https://doi.org/10.1007/s12257-019-0381-2
|
[34]
|
Wang, Y., Luo, X., Zhao, Y., et al. (2021) Integrated Strategies for Enhancing the Expression of the AqCoA Chitosanase in Pichia pastoris by Combined Optimization of Molecular Chaperones Combinations and Copy Numbers via a Novel Plasmid pMC-GAP. Applied Biochemistry and Biotechnology, 193, 4035-4051.
https://doi.org/10.1007/s12010-021-03668-9
|
[35]
|
De Waele, S., Vandenberghe, I., Laukens, B., et al. (2018) Op-timized Expression of the Starmerella bombicola Lactone Esterase in Pichia pastoris through Temperature Adaptation, Codon-Optimization and Co-Expression with HAC1. Protein Expression and Purification, 143, 62-70. https://doi.org/10.1016/j.pep.2017.10.016
|
[36]
|
Gasser, B., Maurer, M., Gach, J., et al. (2006) Engineering of Pichia pastoris for Improved Production of Antibody Fragments. Biotechnology and Bioengineering, 94, 353-361. https://doi.org/10.1002/bit.20851
|
[37]
|
Krainer, F.W., Gerstmann, M.A., Darnhofer, B., et al. (2016) Biotechnolog-ical Advances towards an Enhanced Peroxidase Production in Pichia pastoris. Journal of Biotechnology, 233, 181-189.
https://doi.org/10.1016/j.jbiotec.2016.07.012
|
[38]
|
Lin, X.Q., Liang, S.L., Han, S.Y., et al. (2013) Quantitative iTRAQ LC-MS/MS Proteomics Reveals the Cellular Response to Heterologous Protein Overexpression and the Regula-tion of HAC1 in Pichia pastoris. Journal of Proteomics, 2013, 91, 58-72. https://doi.org/10.1016/j.jprot.2013.06.031
|
[39]
|
Huang, M., Gao, Y., Zhou, X., et al.(2017) Regulating Unfolded Protein Response Activator HAC1p for Production of Thermostable Raw-Starch Hydrolyzing α-Amylase in Pichia pas-toris. Bioprocess and Biosystems Engineering, 40, 341-350. https://doi.org/10.1007/s00449-016-1701-y
|
[40]
|
Bankefa, O.E., Wang, M., Zhu, T., et al. (2018) Hac1p Homo-logues from Higher Eukaryotes Can Improve the Secretion of Heterologous Proteins in the Yeast Pichia pastoris. Bio-technology Letters, 40, 1149-1156.
https://doi.org/10.1007/s10529-018-2571-y
|
[41]
|
Kruse, K.B., Brodsky, J.L. and McCracken, A.A. (2006) Au-tophagy: An ER Protein Quality Control Process. Autophagy, 2, 135-137. https://doi.org/10.4161/auto.2.2.2388
|
[42]
|
Liu, J., Han, Q., Cheng, Q., et al. (2020) Efficient Expression of Human Lysozyme through the Increased Gene Dosage and Co-Expression of Transcription Factor Hac1p in Pichia pastoris. Current Microbiology, 77, 846-854.
https://doi.org/10.1007/s00284-019-01872-9
|
[43]
|
Liu, X., Wu, D., Wu, J., et al. (2013) Optimization of the Pro-duction of Aspergillus niger α-Glucosidase Expressed in Pichia pastoris. World Journal of Microbiology & Biotechnol-ogy, 29, 533-540.
https://doi.org/10.1007/s11274-012-1207-y
|
[44]
|
Whyteside, G., Alcocer, M.J., Kumita, J.R., et al. (2011) Na-tive-State Stability Determines the Extent of Degradation Relative to Secretion of Protein Variants from Pichia pastoris. PLOS ONE, 6, e22692.
https://doi.org/10.1371/journal.pone.0022692
|