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Journal articles on the topic 'Pichia pastoria'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Lahoz, Carlos, Isabel Cortegano, Ascensión Minguez, et al. "Cup a 3, major allergen from Cupressus arizonica: Cloning and expression in pichia pastoria." Journal of Allergy and Clinical Immunology 109, no. 1 (2002): S136—S137. http://dx.doi.org/10.1016/s0091-6749(02)81533-0.

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2

Martius, Efrida, Andree Triyadi, Dewi Yustika Sofia, and Anis Herliyati Mahsunah. "PENGARUH VARIASI KONSENTRASI METANOL DAN LAMA INDUKSI TERHADAP EKSPRESI PROINSULIN OLEH Pichia pastoris SECARA INTRASELULER." Jurnal Bioteknologi & Biosains Indonesia (JBBI) 6, no. 1 (2019): 93. http://dx.doi.org/10.29122/jbbi.v6i1.3176.

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The Effects of Variation in Methanol Concentration and Induction Time on Intracellular Proinsulin Expression by Pichia pastoris ABSTRACTDiabetes is a metabolic disorder characterized by hyperglycemia. There were 215 million diabetic patients in 2014 and the number is expected to rise in 2040. Generally, insulin is used to treat diabetic patients. Insulin production by recombinant technology has been done, though still inefficient, by using E. coli and S. cerevisiae expression system. Another alternative expression system is methylotrophic yeast Pichia pastoris. In this research, proinsulin has

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3

Borshchevskaya, L. N., T. L. Gordeeva та S. P. Sineoky. "Increase in the Production of Endo-1,4-β-Xylanase from Paenibacillus brasilensis in Pichia pastoris". Biotekhnologiya 35, № 6 (2019): 30–38. http://dx.doi.org/10.21519/0234-2758-2019-35-6-30-38.

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A Pichia pastoris yeast strain producing endo-l,4-β-xylanase from Paenibacillus brasilensis with an activity of 54,400 U/mL after 140 h of fermentation in a laboratory fermenter has been obtained. A number of approaches were used to increase the level of the xylanase production in this strain: optimization of the target gene codon composition, multiple integration of the expression cassette into the recipient strain chromosome using the Cre-lox recombination system, and also improving the heterologous protein folding via the overexpression of the HAC1i gene from Pichia pastoris. xylanase, xyla

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4

Sheina, N. I., J. G. Skryabina, L. I. Myalina та ін. "MICROORGANISM BACILLUS KOMAGATAELLA (PICHIA) PASTORIS ВKПМ Y-4225". Toxicological Review, № 1 (28 лютого 2017): 58–60. http://dx.doi.org/10.36946/0869-7922-2017-1-58-60.

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Hazard and toxicity assessment of the microorganism Bacillus Komagataella (Pichia)pastoris ВKПМ Y-4225 was performed. In accordance with legislative regulatory documents in force for its congener in taxonomic aspect of cytochrome C producer strain Pichia membranifaciens ВKПМ Y-934, MAC occupational air on the level of 2x103 cells/m3 mark A and MAC atmospheric air on the level of 2x102 cells/m3 mark A in residential settings are recommended for the microorganism Bacillus Komagataella (Pichia) pastoris ВKПМ Y-4225.

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5

Bae, Kyung-Dong. "Expression of Δ-desaturase Gene in a Recombinant Pichia pastoris GS115 Strain and Its Activity". KSBB Journal 26, № 6 (2011): 557–60. http://dx.doi.org/10.7841/ksbbj.2011.26.6.557.

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6

Borshchevskaya, L. N., A. N. Kalinina, S. P. Sineoky, and M. D. Kashirskaya. "Effect of Overexpression of the HAC1 Genes from Pichia pastoris and Saccharomyces cerevisiae on the Heterologous Phytase and Xylanase Production by P. pastoris." Biotekhnologiya 35, no. 6 (2019): 57–66. http://dx.doi.org/10.21519/0234-2758-2019-35-6-57-66.

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Effect of overexpression of the HAC1 genes from Pichia pastoris and Saccharomyces cerevisiae on the production of heterologous enzymes, Escherichia coli phytase and Paenibacillus brasilensis xylanase, in P. pastoris cells has been studied. Codon composition of the phytase and xylanase encoding genes was optimized, and the genes were expressed in P. pastoris under the control of AOX1 promoter. The obtained multi-copy strains produced in vitro 927 U/mL phytase and 1,401 U/ml xylanase activity. Overexpression of the HAC1 gene from P. pastoris was shown to increase the phytase and xylanase product

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7

Lazareva, M. N., E. I. Semenko та S. P. Sineoky. "Expression of Aspergillus aculeatus β-mannanase in Pichia pastoris Yeast and Analysis of Industrially Important Properties of Enzyme". Biotekhnologiya 35, № 1 (2019): 38–44. http://dx.doi.org/10.21519/0234-2758-2019-35-1-38-44.

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β-Mannanases are enzymes for the industrial application and they can be used, in particular, in the feed industry. The most important requirements for feed enzymes are broad pH range, thermal stability and high specific activity. The efficient expression of the man1 gene encoding Aspergillus aculeatus β-1,4-mannanases in Pichia pastoris yeast cells has been obtained for the first time. The industrially valuable properties of the enzyme were confirmed. The obtained data indicate that the man1 gene from A. aculeatus is potentially useful for the construction of industrial mannanase producers on

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8

Yadava, Anjali, and Christian F. Ockenhouse. "Effect of Codon Optimization on Expression Levels of a Functionally Folded Malaria Vaccine Candidate in Prokaryotic and Eukaryotic Expression Systems." Infection and Immunity 71, no. 9 (2003): 4961–69. http://dx.doi.org/10.1128/iai.71.9.4961-4969.2003.

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ABSTRACT We have produced two synthetic genes that code for the F2 domain located within region II of the 175-kDa Plasmodium falciparum erythrocyte binding antigen (EBA-175) to determine the effects of codon alteration on protein expression in homologous and heterologous host systems. EBA-175 plays a key role in the process of merozoite invasion into erythrocytes through a specific receptor-ligand interaction. The F2 domain of EBA-175 is the ligand that binds to the glycophorin A receptor on human erythrocytes and is therefore a target of vaccine development efforts. We designed synthetic gene

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9

Peña, David A., Brigitte Gasser, Jürgen Zanghellini, Matthias G. Steiger, and Diethard Mattanovich. "Metabolic engineering of Pichia pastoris." Metabolic Engineering 50 (November 2018): 2–15. http://dx.doi.org/10.1016/j.ymben.2018.04.017.

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10

Gasser, Brigitte. "Systems biology of Pichia pastoris." New Biotechnology 31 (July 2014): S3—S4. http://dx.doi.org/10.1016/j.nbt.2014.05.1621.

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11

Cregg, J. M., K. J. Barringer, A. Y. Hessler, and K. R. Madden. "Pichia pastoris as a host system for transformations." Molecular and Cellular Biology 5, no. 12 (1985): 3376–85. http://dx.doi.org/10.1128/mcb.5.12.3376.

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We developed a methylotrophic yeast, Pichia pastoris, as a host for DNA transformations. The system is based on an auxotrophic mutant host of P. pastoris which is defective in histidinol dehydrogenase. As a selectable marker, we isolated and characterized the P. pastoris HIS4 gene. Plasmid vectors which contained either the P. pastoris or the Saccharomyces cerevisiae HIS4 gene transformed the P. pastoris mutant host. DNA transfer was accomplished by a modified version of the spheroplast generation (CaCl2-polyethylene glycol)-fusion procedure developed for S. cerevisiae. In addition, we report

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12

Cregg, J. M., K. J. Barringer, A. Y. Hessler, and K. R. Madden. "Pichia pastoris as a host system for transformations." Molecular and Cellular Biology 5, no. 12 (1985): 3376–85. http://dx.doi.org/10.1128/mcb.5.12.3376-3385.1985.

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We developed a methylotrophic yeast, Pichia pastoris, as a host for DNA transformations. The system is based on an auxotrophic mutant host of P. pastoris which is defective in histidinol dehydrogenase. As a selectable marker, we isolated and characterized the P. pastoris HIS4 gene. Plasmid vectors which contained either the P. pastoris or the Saccharomyces cerevisiae HIS4 gene transformed the P. pastoris mutant host. DNA transfer was accomplished by a modified version of the spheroplast generation (CaCl2-polyethylene glycol)-fusion procedure developed for S. cerevisiae. In addition, we report

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13

Gordeeva, T. L., L. N. Borshchevskaya, A. N. Kalinina, S. P. Sineoky, S. P. Voronin, and M. D. Kashirskaya. "Expression and Characteristics of Phytases from Obesumbacterium proteus in Pichia pastoris Yeast." Biotekhnologiya 34, no. 4 (2018): 18–25. http://dx.doi.org/10.21519/0234-2758-2018-34-4-18-25.

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14

Shao, Jun, Takahisa Hayashi та Peng George Wang. "Enhanced Production of α-Galactosyl Epitopes by Metabolically Engineered Pichia pastoris". Applied and Environmental Microbiology 69, № 9 (2003): 5238–42. http://dx.doi.org/10.1128/aem.69.9.5238-5242.2003.

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ABSTRACT A metabolically engineered Pichia pastoris strain was constructed that harbored three heterologous enzymes: an S11E mutated sucrose synthase from Vigna radiata, a truncated UDP-glucose C4 epimerase from Saccharomyces cerevisiae, and a truncated bovine α-1,3-galactosyltransferase. Each gene has its own methanol-inducible alcohol oxidase 1 promoter and transcription terminator on the chromosomal DNA of P. pastoris strain GS115. The proteins were coexpressed intracellularly under the induction of methanol. After permeabilization, the whole P. pastoris cells were used to synthesize α-gala

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15

Jin, Xuerong, Weijiao Zhang, Yang Wang, et al. "Biosynthesis of non-animal chondroitin sulfate from methanol using genetically engineered Pichia pastoris." Green Chemistry 23, no. 12 (2021): 4365–74. http://dx.doi.org/10.1039/d1gc00260k.

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16

Huang, Wenjing, Yanjie Tong, Wangxiang Huang, et al. "Influence of 1-butyl-3-methylimidazolium Chloride on the Ethanol Fermentation Process of Pichia pastoris GS115." Open Biotechnology Journal 9, no. 1 (2015): 109–12. http://dx.doi.org/10.2174/1874070701509010109.

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To evaluate the influence of 1-butyl-3-methylimidazolium chloride ([Bmim]Cl) on the ethanol fermentation process of Pichia pastoris GS115, this paper investigated the yeast growth, ethanol formation and the fermentable sugars consumption during the ethanol fermentation process of Pichia pastoris GS115 at different [Bmim]Cl concentrations in the medium. The results indicated that the [Bmim]Cl had no influence on the ethanol fermentation process at its concentration less than 0.0001 g.L-1. The [Bmim]Cl inhibited the yeast growth and had a negative effect on ethanol formation at its concentration

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17

Modak, J., and K. Konde. "Multiobjective optimization of Pichia pastoris fermentations." New Biotechnology 25 (September 2009): S241. http://dx.doi.org/10.1016/j.nbt.2009.06.233.

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18

Cregg, James M., Joan Lin Cereghino, Jianying Shi, and David R. Higgins. "Recombinant Protein Expression in Pichia pastoris." Molecular Biotechnology 16, no. 1 (2000): 23–52. http://dx.doi.org/10.1385/mb:16:1:23.

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19

Dietzsch, C., and C. Herwig. "Bioprozessoptimierung eines rekombinanten Pichia pastoris-Expressionsstammes." Chemie Ingenieur Technik 82, no. 9 (2010): 1494–95. http://dx.doi.org/10.1002/cite.201050397.

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20

Kottmeier, K., K. Ostermann, T. Bley, and G. Rödel. "Herstellung von Hydrophobinen in Pichia pastoris." Chemie Ingenieur Technik 82, no. 9 (2010): 1545. http://dx.doi.org/10.1002/cite.201050439.

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21

Vogl, Thomas, Claudia Ruth, Julia Pitzer, Thomas Kickenweiz, and Anton Glieder. "Synthetic Core Promoters for Pichia pastoris." ACS Synthetic Biology 3, no. 3 (2013): 188–91. http://dx.doi.org/10.1021/sb400091p.

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22

Vedvick, Thomas S. "Gene expression in yeast: Pichia pastoris." Current Opinion in Biotechnology 2, no. 5 (1991): 742–45. http://dx.doi.org/10.1016/0958-1669(91)90045-7.

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23

Guerrero-Olazarán, Martha, Lilí Rodríguez-Blanco, Jesús G. Carreon-Treviño, Juan A. Gallegos-López, Miguel Castillo-Galván, and José M. Viader-Salvadó. "Bacterial phytase produced in Pichia pastoris." Journal of Biotechnology 131, no. 2 (2007): S233—S234. http://dx.doi.org/10.1016/j.jbiotec.2007.07.425.

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24

Sturmberger, Lukas, Thomas Chappell, Martina Geier, et al. "Refined Pichia pastoris reference genome sequence." Journal of Biotechnology 235 (October 2016): 121–31. http://dx.doi.org/10.1016/j.jbiotec.2016.04.023.

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25

He, Li Yan, Gui Bin Wang, Fu Liang Cao, Lin Guo Zhao, and Yong Xin Ji. "Cloning of Laccase Gene from Coriolus Versicolor and Optimization of Culture Conditions for Lcc1 Expression in Pichia Pastoris." Advanced Materials Research 236-238 (May 2011): 1039–44. http://dx.doi.org/10.4028/www.scientific.net/amr.236-238.1039.

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A laccase cDNA lcc1 (GenBank accession number HM137002), without native signal peptide, was cloned by RT-PCR from total RNA of Coriolus versicolor. Recombination expression vector pPICZαA-lcc1 was constructed and transformed into Pichia pastoris KM71H after lineared. Recombination laccase was expressed at a higher level. Single factors of fermentation conditions of Pichia pastoris KM71H for laccase production were optimized. The results showed optimal culture conditions were as follows: medium initial pH 7.5, Cu2+ concentration 0.5mmol/L, methanol additive amount 1.0% and shaker rotate speed 2

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26

Cregg, James M., and David R. Higgins. "Production of foreign proteins in the yeast Pichia pastoris." Canadian Journal of Botany 73, S1 (1995): 891–97. http://dx.doi.org/10.1139/b95-336.

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The methanol-utilizing yeast Pichia pastoris has been developed as a host system for the production of heterologous proteins of commercial interest. An industrial yeast selected for efficient growth on methanol for biomass generation, P. pastoris is readily grown on defined medium in continuous culture at high volume and density. A unique feature of the expression system is the promoter employed to drive heterologous gene expression, which is derived from the methanol-regulated alcohol oxidase I gene (AOX1) of P. pastoris, one of the most efficient and tightly regulated promoters known. The st

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27

Strauss, C. E., T. A. McAllister, and L. B. Selinger. "Development of Pichia pastoris as a rumen escape vehicle for the intestinal delivery of recombinant proteins in ruminants." Canadian Journal of Animal Science 84, no. 4 (2004): 611–19. http://dx.doi.org/10.4141/a03-097.

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The effectiveness of cellular encapsulation as a method for delivery of bioactive proteins and limiting amino acids to the small intestine of ruminants was investigated. Intracellular expression of green fluorescent protein variant (GFPuv) in Pichia pastoris was used as a visible marker to assess the cellular integrity of P. pastoris and determine the potential of this approach for protecting recombinant proteins from microbial proteolysis in the rumen. Fluorescent cells were easily identified in the presence of strained ruminal fluid when viewed by epifluorescent microscopy, and intact cells

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28

Vervecken, Wouter, Vladimir Kaigorodov, Nico Callewaert, Steven Geysens, Kristof De Vusser, and Roland Contreras. "In Vivo Synthesis of Mammalian-Like, Hybrid-Type N-Glycans in Pichia pastoris." Applied and Environmental Microbiology 70, no. 5 (2004): 2639–46. http://dx.doi.org/10.1128/aem.70.5.2639-2646.2004.

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ABSTRACT The Pichia pastoris N-glycosylation pathway is only partially homologous to the pathway in human cells. In the Golgi apparatus, human cells synthesize complex oligosaccharides, whereas Pichia cells form mannose structures that can contain up to 40 mannose residues. This hypermannosylation of secreted glycoproteins hampers the downstream processing of heterologously expressed glycoproteins and leads to the production of protein-based therapeutic agents that are rapidly cleared from the blood because of the presence of terminal mannose residues. Here, we describe engineering of the P. p

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29

Zhang, Qiu-Hua, Liu Yang, Yi-Bin Tang, Liu-Nv Huang, and Wen-Fang Luo. "Industrial kinetic resolution of d,l-pantolactone by an immobilized whole-cell biocatalyst." RSC Advances 11, no. 48 (2021): 30373–76. http://dx.doi.org/10.1039/d1ra05708a.

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Immobilized whole-cells of Pichia pastoris harboring recombinant d-lactonase were entrapped in calcium alginate gels and used as an efficient biocatalyst for catalytic kinetic resolution of d,l-pantolactone.

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30

Robles-Zamora, A., D. Enriquez-Ochoa, M. Ureña-Herrera, J. M. Aguilar-Yañez, M. E. G. Brunck, and K. Mayolo-Deloisa. "Partial recovery of MRJP1 protein expressed in Pichia pastoris using chromatographic techniques." Revista Mexicana de Ingeniería Química 20, no. 1 (2020): 147–61. http://dx.doi.org/10.24275/rmiq/bio1713.

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31

Borschevskaya, L. N., T. L. Gordeeva, and S. P. Sineoky. "Expression of Xylanase Gene from Pyromyces finnis in Pichia pastoris and Characterization of Recombinant Protein." Biotekhnologiya 35, no. 4 (2019): 24–32. http://dx.doi.org/10.21519/0234-2758-2019-35-4-24-32.

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The heterologous expression and characteristics of a new xylanase from Pyromyces finnis have been described. The endo-l,4-β-xylanase XylP (EC 3.2.1.8) consists of 223 amino acids and 19 residues of a putative signal peptide in the N-terminal region. The amino acid sequence of the mature protein has the greatest homology with the sequence of the native catalytic N-terminal domain of Neocallimastix patriciarum endo-l,4-β-xylanase (84%). A synthetic nucleotide sequence encoding a mature XylP protein was expressed in Pichia pastoris. The purified recombinant enzyme showed activity with birch xylan

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32

Pham, Vu Minh, Huy Hua Hoang Quoc, Huong-Xuan Mai Le, and Tri-Nhan Nguyen*. "Storage of the Recombinant Protein hPDGF-BB in the Culture of Pichia pastoris." International Journal of Life-Sciences Scientific Research 4, no. 4 (2018): 1934–39. http://dx.doi.org/10.21276/ijlssr.2018.4.4.11.

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33

Ndayambaje, Jean Bernard, Gratien Habarurema, Janvier Habinshuti, et al. "Integration of GC-MS in identification of possible final metabolites from phytase production in Pichia Pastoris based on sorbitol induction optimization." Archives of Biotechnology and Biomedicine 5, no. 1 (2021): 020–25. http://dx.doi.org/10.29328/journal.abb.1001024.

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The isolation of phytase using Pichia Pastoris under methanol/sorbitol co-feeding induction technique was investigated. The biological activity of extracellular phytase after optimization with co-substrates induction in 4 liters fermentor (NBS) increased to 13250 U/ml. This led to a 509 fold increases in comparison to the other type of phytase. This effect was studied via induction with sorbitol/methanol in fermentation by Pichia Pastoris GS115 (Mut+) at 20 °C. The interference of by products; methylal, hexamine and (S)-(+)-1,2-propanediol with release of phytase in Pichia Pastoris under metha

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34

Nurdiani, Dini, Hariyatun Hariyatun та Wien Kusharyoto. "Secretory expression of human insulin precursor in Pichia pastoris employing truncated α-factor leader sequence and a short C-peptide". Indonesian Journal of Biotechnology 23, № 2 (2018): 102. http://dx.doi.org/10.22146/ijbiotech.38958.

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In the past ten years, diabetes prevalence has increased rapidly in low- and middle-income countries due to lifestyle changes. This increased number of diabetic patients leads to the escalation of recombinant insulin demand, which is creating a large global insulin market. Pichia pastoris has appeared as an alternative host to produce recombinant proteins. It has excellent qualifications as an expression host for large-scale production of recombinant proteins for therapeutic use. In this study, we attempted to express the insulin precursor (IP) in P. pastoris. We used a synthetic IP-encoding g

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35

Bridges, Hannah R., Ljuban Grgic, Michael E. Harbour, and Judy Hirst. "The respiratory complexes I from the mitochondria of two Pichia species." Biochemical Journal 422, no. 1 (2009): 151–59. http://dx.doi.org/10.1042/bj20090492.

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NADH:ubiquinone oxidoreductase (complex I) is an entry point for electrons into the respiratory chain in many eukaryotes. It couples NADH oxidation and ubiquinone reduction to proton translocation across the mitochondrial inner membrane. Because complex I deficiencies occur in a wide range of neuromuscular diseases, including Parkinson's disease, there is a clear need for model eukaryotic systems to facilitate structural, functional and mutational studies. In the present study, we describe the purification and characterization of the complexes I from two yeast species, Pichia pastoris and Pich

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36

Kashirskaya, M. D., M. N. Lazareva, A. R. Lapteva, V. Yu Dobrynin, T. L. Gordeeva, and S. P. Sineoky. "Comparative Characteristics of Phytases from Citrobacter freundii and Yersinia intermedia Expressed in Ogataea polymorpha and Pichia pastoris Methylotrophic Yeasts." Biotekhnologiya 35, no. 6 (2019): 51–56. http://dx.doi.org/10.21519/0234-2758-2019-35-6-51-56.

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The genes for bacterial phytases from Citrobacter freundii and Yersinia intermedia were expressed for the first time in a thermotolarant yeast Ogataea polymorpha. A comparative analysis of the properties of recombinant phytases produced by Ogataea polymorpha and Pichia pastoris yeasts was carried out. It was shown that the stability, pH and temperature profiles of the enzyme activities are the same regardless of the host strain. It was proved that O. polymorpha yeast can be used to create producers of feed enzymes and to develop a technology for their cultivation at temperatures above 37 °C. T

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37

Schwarzhans, Jan-Philipp, Tobias Luttermann, Martina Geier, Jörn Kalinowski, and Karl Friehs. "Towards systems metabolic engineering in Pichia pastoris." Biotechnology Advances 35, no. 6 (2017): 681–710. http://dx.doi.org/10.1016/j.biotechadv.2017.07.009.

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38

DUFF, Sheldon J. B., and William D. MURRAY. "Metabolism of hydrogen peroxide by Pichia pastoris." Agricultural and Biological Chemistry 54, no. 8 (1990): 1967–73. http://dx.doi.org/10.1271/bbb1961.54.1967.

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39

Mellitzer, Andrea, Roland Weis, Anton Glieder, and Karlheinz Flicker. "Expression of lignocellulolytic enzymes in Pichia pastoris." Microbial Cell Factories 11, no. 1 (2012): 61. http://dx.doi.org/10.1186/1475-2859-11-61.

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40

LI, Z., X. YU, J. HUANG, H. FANG, and H. CHEN. "Recombinant Batroxobin Expressed Highly in Pichia pastoris." Chinese Journal of Biotechnology 23, no. 3 (2007): 483–87. http://dx.doi.org/10.1016/s1872-2075(07)60035-1.

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41

Heistinger, Lina, Brigitte Gasser, and Diethard Mattanovich. "Modulating the mating behavior of Pichia pastoris." New Biotechnology 33 (July 2016): S4. http://dx.doi.org/10.1016/j.nbt.2016.06.742.

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42

Potgieter, Thomas I., Sean D. Kersey, Muralidhar R. Mallem, Adam C. Nylen, and Marc d'Anjou. "Antibody expression kinetics in glycoengineered Pichia pastoris." Biotechnology and Bioengineering 106, no. 6 (2010): 918–27. http://dx.doi.org/10.1002/bit.22756.

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43

Schroder, Laura A., and William A. Dunn Jr. "PpAtg9 Trafficking During Micropexophagy in Pichia pastoris." Autophagy 2, no. 1 (2006): 52–54. http://dx.doi.org/10.4161/auto.2200.

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44

Padkina, M. V., L. V. Parfenova, A. E. Gradoboeva, and E. V. Sambuk. "Heterologous interferons synthesis in yeast Pichia pastoris." Applied Biochemistry and Microbiology 46, no. 4 (2010): 409–14. http://dx.doi.org/10.1134/s0003683810040083.

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45

Kern, Alexander, Franz S. Hartner, Maria Freigassner, et al. "Pichia pastoris ‘just in time’ alternative respiration." Microbiology 153, no. 4 (2007): 1250–60. http://dx.doi.org/10.1099/mic.0.2006/001404-0.

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46

Buyuksungur, Arda, and Pinar Calik. "Extracellular benzaldehyde lyase production by Pichia pastoris." Journal of Biotechnology 131, no. 2 (2007): S175—S176. http://dx.doi.org/10.1016/j.jbiotec.2007.07.911.

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47

Kerr, Heather, Andy H. Herbert, A. Richards, and Paul N. Barlow. "Recombinant mouse factor H from Pichia pastoris." Immunobiology 217, no. 11 (2012): 1198. http://dx.doi.org/10.1016/j.imbio.2012.08.197.

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48

Li, Pingzuo, Anukanth Anumanthan, Xiu-Gong Gao, et al. "Expression of Recombinant Proteins in Pichia Pastoris." Applied Biochemistry and Biotechnology 142, no. 2 (2007): 105–24. http://dx.doi.org/10.1007/s12010-007-0003-x.

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Boys, C. W. G., D. J. Hill, P. G. Stockley, and J. R. Woodward. "Crystallization of alcohol oxidase from Pichia pastoris." Journal of Molecular Biology 208, no. 1 (1989): 211–12. http://dx.doi.org/10.1016/0022-2836(89)90099-5.

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Hagenson, M. J., K. A. Holden, K. A. Parker, et al. "Expression of streptokinase in Pichia pastoris yeast." Enzyme and Microbial Technology 11, no. 10 (1989): 650–56. http://dx.doi.org/10.1016/0141-0229(89)90003-3.

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