Comparative evaluation of the extracellular production of a polyethylene terephthalate degrading cutinase by Corynebacterium glutamicum and leaky Escherichia coli in batch and fed-batch processes.
Autoinduction
Bioreactor
Cutinase
Enzymatic depolymerization
Extracellular
Lactose feed
Polyethylene terephthalate
Recombinant protein expression
Secretion
Journal
Microbial cell factories
ISSN: 1475-2859
Titre abrégé: Microb Cell Fact
Pays: England
ID NLM: 101139812
Informations de publication
Date de publication:
10 Oct 2024
10 Oct 2024
Historique:
received:
26
06
2024
accepted:
30
09
2024
medline:
11
10
2024
pubmed:
11
10
2024
entrez:
10
10
2024
Statut:
epublish
Résumé
With a growing global population, the generation of plastic waste and the depletion of fossil resources are major concerns that need to be addressed by developing sustainable and efficient plastic recycling methods. Biocatalytic recycling is emerging as a promising ecological alternative to conventional processes, particularly in the recycling of polyethylene terephthalate (PET). However, cost-effective production of the involved biocatalyst is essential for the transition of enzymatic PET recycling to a widely used industrial technology. Extracellular enzyme production using established organisms such as Escherichia coli or Corynebacterium glutamicum offers a promising way to reduce downstream processing costs. In this study, we compared extracellular recombinant protein production by classical secretion in C. glutamicum and by membrane leakage in E. coli. A superior extracellular release of the cutinase ICCG Extracellular production can reduce the cost of recombinant proteins by simplifying downstream processing. In the case of the PET-hydrolysing cutinase ICCG
Sections du résumé
BACKGROUND
BACKGROUND
With a growing global population, the generation of plastic waste and the depletion of fossil resources are major concerns that need to be addressed by developing sustainable and efficient plastic recycling methods. Biocatalytic recycling is emerging as a promising ecological alternative to conventional processes, particularly in the recycling of polyethylene terephthalate (PET). However, cost-effective production of the involved biocatalyst is essential for the transition of enzymatic PET recycling to a widely used industrial technology. Extracellular enzyme production using established organisms such as Escherichia coli or Corynebacterium glutamicum offers a promising way to reduce downstream processing costs.
RESULTS
RESULTS
In this study, we compared extracellular recombinant protein production by classical secretion in C. glutamicum and by membrane leakage in E. coli. A superior extracellular release of the cutinase ICCG
CONCLUSION
CONCLUSIONS
Extracellular production can reduce the cost of recombinant proteins by simplifying downstream processing. In the case of the PET-hydrolysing cutinase ICCG
Identifiants
pubmed: 39390488
doi: 10.1186/s12934-024-02547-2
pii: 10.1186/s12934-024-02547-2
doi:
Substances chimiques
Polyethylene Terephthalates
0
cutinase
EC 3.1.1.-
Carboxylic Ester Hydrolases
EC 3.1.1.-
Recombinant Proteins
0
Types de publication
Journal Article
Comparative Study
Langues
eng
Sous-ensembles de citation
IM
Pagination
274Informations de copyright
© 2024. The Author(s).
Références
Brahney J, Hallerud M, Heim E, Hahnenberger M, Sukumaran S. Plastic rain in protected areas of the United States. Science. 1979;2020(368):1257–60.
Eriksen M, Lebreton LCM, Carson HS, Thiel M, Moore CJ, Borerro JC, et al. Plastic pollution in the world’s oceans: more than 5 trillion plastic pieces weighing over 250,000 tons afloat at sea. PLoS ONE. 2014;9: e111913.
pubmed: 25494041
pmcid: 4262196
doi: 10.1371/journal.pone.0111913
Urbanek AK, Kosiorowska KE, Mirończuk AM. Current knowledge on polyethylene terephthalate degradation by genetically modified microorganisms. Front Bioeng Biotechnol. 2021;9(9):771133.
pubmed: 34917598
pmcid: 8669999
doi: 10.3389/fbioe.2021.771133
Nisticò R. Polyethylene terephthalate (PET) in the packaging industry. Polym Test. 2020;90:106707.
doi: 10.1016/j.polymertesting.2020.106707
Kawai F. The current state of research on PET hydrolyzing enzymes available for biorecycling. Catalysts. 2021;11:206.
doi: 10.3390/catal11020206
Xu A, Zhou J, Blank LM, Jiang M. Future focuses of enzymatic plastic degradation. Trends Microbiol. 2023;31:668–71.
pubmed: 37121829
doi: 10.1016/j.tim.2023.04.002
Satta A, Zampieri G, Loprete G, Campanaro S, Treu L, Bergantino E. Metabolic and enzymatic engineering strategies for polyethylene terephthalate degradation and valorization. Rev Environ Sci Biotechnol. 2024;23:351–83.
doi: 10.1007/s11157-024-09688-1
Tournier V, Duquesne S, Guillamot F, Cramail H, Taton D, Marty A, et al. Enzymes’ power for plastics degradation. Chem Rev. 2023;123:5612–701.
pubmed: 36916764
doi: 10.1021/acs.chemrev.2c00644
Arnal G, Anglade J, Gavalda S, Tournier V, Chabot N, Bornscheuer UT, et al. Assessment of four engineered pet degrading enzymes considering large-scale industrial applications. ACS Catal. 2023;13:13156–66.
pubmed: 37881793
pmcid: 10594578
doi: 10.1021/acscatal.3c02922
Fritzsche S, Tischer F, Peukert W, Castiglione K. You get what you screen for: a benchmark analysis of leaf branch compost cutinase variants for polyethylene terephthalate (PET) degradation. React Chem Eng. 2023;8:2156–69.
doi: 10.1039/D3RE00056G
Decker JS, Menacho-Melgar R, Lynch MD. Low-cost, large-scale production of the anti-viral Lectin Griffithsin. Front Bioeng Biotechnol. 2020. https://doi.org/10.3389/fbioe.2020.01020 .
doi: 10.3389/fbioe.2020.01020
pubmed: 32974328
pmcid: 7471252
Hatti-Kaul R. Downstream processing in industrial biotechnology. In: Industrial biotechnology. Hoboken: Wiley; 2010. p. 279–321.
doi: 10.1002/9783527630233.ch8
Singh N, Herzer S. Downstream processing technologies/capturing and final purification. Cham: Springer International Publishing; 2017. p. 115–78.
Yoshida S, Hiraga K, Taniguchi I, Oda K. Ideonella sakaiensis, PETase, and MHETase: from identification of microbial PET degradation to enzyme characterization. Methods Enzymol. 2021;648:187–205.
pubmed: 33579403
doi: 10.1016/bs.mie.2020.12.007
Yoshida S, Hiraga K, Takehana T, Taniguchi I, Yamaji H, Maeda Y, et al. A bacterium that degrades and assimilates poly(ethylene terephthalate). Science. 1979;2016(351):1196–9.
Shirke AN, White C, Englaender JA, Zwarycz A, Butterfoss GL, Linhardt RJ, et al. Stabilizing leaf and branch compost cutinase (LCC) with glycosylation: mechanism and effect on PET hydrolysis. Biochemistry. 2018;57:1190–200.
pubmed: 29328676
doi: 10.1021/acs.biochem.7b01189
Oh Y-R, Jang Y-A, Song JK, Eom GT. Secretory production of an engineered cutinase in Bacillus subtilis for efficient biocatalytic depolymerization of polyethylene terephthalate. Bioprocess Biosyst Eng. 2022;45:711–20.
pubmed: 35039943
doi: 10.1007/s00449-022-02690-3
Liu X-X, Li Y, Bai Z-H. Corynebacterium glutamicum as a robust microbial factory for production of value-added proteins and small molecules: fundamentals and applications. In: Microbial Cell factories engineering for production of biomolecules. Amsterdam: Elsevier; 2021. p. 235–63.
doi: 10.1016/B978-0-12-821477-0.00006-4
Helleckes LM, Müller C, Griesbach T, Waffenschmidt V, Moch M, Osthege M, et al. Explore or exploit? A model-based screening strategy for PETase secretion by Corynebacterium glutamicum. Biotechnol Bioeng. 2023;120:139–53.
pubmed: 36225165
doi: 10.1002/bit.28261
Hemmerich J, Rohe P, Kleine B, Jurischka S, Wiechert W, Freudl R, et al. Use of a Sec signal peptide library from Bacillus subtilis for the optimization of cutinase secretion in Corynebacterium glutamicum. Microb Cell Fact. 2016;15:208.
pubmed: 27927208
pmcid: 5142396
doi: 10.1186/s12934-016-0604-6
Soong YV, Abid U, Chang AC, Ayafor C, Patel A, Qin J, et al. Enzyme selection, optimization, and production toward biodegradation of post-consumer poly(ethylene terephthalate) at scale. Biotechnol J. 2023. https://doi.org/10.1002/biot.202300119 .
doi: 10.1002/biot.202300119
pubmed: 37594123
Sulaiman S, Yamato S, Kanaya E, Kim J-J, Koga Y, Takano K, et al. Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach. Appl Environ Microbiol. 2012;78:1556–62. https://doi.org/10.1128/AEM.06725-11 .
doi: 10.1128/AEM.06725-11
pubmed: 22194294
pmcid: 3294458
Su L, Woodard RW, Chen J, Wu J. Extracellular location of Thermobifida fusca cutinase expressed in Escherichia coli BL21(DE3) without mediation of a signal peptide. Appl Environ Microbiol. 2013;79:4192–8.
pubmed: 23603671
pmcid: 3697513
doi: 10.1128/AEM.00239-13
Yan F, Wei R, Cui Q, Bornscheuer UT, Liu Y. Thermophilic whole-cell degradation of polyethylene terephthalate using engineered Clostridium thermocellum. Microb Biotechnol. 2021;14:374–85.
pubmed: 32343496
doi: 10.1111/1751-7915.13580
Su L, Hong R, Wu J. Enhanced extracellular expression of gene-optimized Thermobifida fusca cutinase in Escherichia coli by optimization of induction strategy. Process Biochem. 2015;50:1039–46.
doi: 10.1016/j.procbio.2015.03.023
Sulaiman S, Yamato S, Kanaya E, Kim J-J, Koga Y, Takano K, et al. Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach. Appl Environ Microbiol. 2012;78:1556–62.
pubmed: 22194294
pmcid: 3294458
doi: 10.1128/AEM.06725-11
Tournier V, Topham CM, Gilles A, David B, Folgoas C, Moya-Leclair E, et al. An engineered PET depolymerase to break down and recycle plastic bottles. Nature. 2020;580:216–9.
pubmed: 32269349
doi: 10.1038/s41586-020-2149-4
Kinoshita S, Nakayama K, Akita S. Taxonomical study of glutamic acid accumulating bacteria Micrococcus glutamicus nov. sp. Bull Agric Chem Soc Japan. 1958;22:176–85.
Tauch A, Kirchner O, Wehmeier L, Kalinowski J, Pühler A. Corynebacterium glutamicum DNA is subjected to methylation-restriction in Escherichia coli. FEMS Microbiol Lett. 1994;123:343–7.
pubmed: 7988915
doi: 10.1111/j.1574-6968.1994.tb07246.x
Müller C, Bakkes PJ, Lenz P, Waffenschmidt V, Helleckes LM, Jaeger K-E, et al. Accelerated strain construction and characterization of C. glutamicum protein secretion by laboratory automation. Appl Microbiol Biotechnol. 2022;106:4481–97.
pubmed: 35759036
pmcid: 9259529
doi: 10.1007/s00253-022-12017-7
Studier FW. Protein production by auto-induction in high-density shaking cultures. Protein Expr Purif. 2005;41:207–34.
pubmed: 15915565
doi: 10.1016/j.pep.2005.01.016
Link H, Anselment B, Weuster-Botz D. Leakage of adenylates during cold methanol/glycerol quenching of Escherichia coli. Metabolomics. 2008;4:240–7.
doi: 10.1007/s11306-008-0114-6
Jenzsch M, Gnoth S, Beck M, Kleinschmidt M, Simutis R, Lübbert A. Open-loop control of the biomass concentration within the growth phase of recombinant protein production processes. J Biotechnol. 2006;127:84–94.
pubmed: 16962679
doi: 10.1016/j.jbiotec.2006.06.004
Georgescu PR. H3K36-dependent anchoring of the KAT Mst2C is required to maintain the balance between euchromatic and heterochromatic domains in S. pombe. Munich: Ludwig-Maximilian-University Munich; 2020.
Schneider CA, Rasband WS, Eliceiri KW. NIH Image to ImageJ: 25 years of image analysis. Nat Methods. 2012;9:671–5.
pubmed: 22930834
pmcid: 5554542
doi: 10.1038/nmeth.2089
Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins MR, Appel RD, et al. Protein identification and analysis tools on the ExPASy server. In: The proteomics protocols handbook. Totowa: Humana Press; 2005. p. 571–607.
doi: 10.1385/1-59259-890-0:571
Bhunia RK, Showman LJ, Jose A, Nikolau BJ. Combined use of cutinase and high-resolution mass-spectrometry to query the molecular architecture of cutin. Plant Methods. 2018;14:117.
pubmed: 30603042
pmcid: 6306009
doi: 10.1186/s13007-018-0384-6
Kleiner-Grote GRM, Risse JM, Friehs K. Secretion of recombinant proteins from E. coli. Eng Life Sci. 2018;18:532–50.
pubmed: 32624934
pmcid: 6999260
doi: 10.1002/elsc.201700200
Stiefel P, Schmidt-Emrich S, Maniura-Weber K, Ren Q. Critical aspects of using bacterial cell viability assays with the fluorophores SYTO9 and propidium iodide. BMC Microbiol. 2015;15:36.
pubmed: 25881030
pmcid: 4337318
doi: 10.1186/s12866-015-0376-x
Boulos L, Prévost M, Barbeau B, Coallier J, Desjardins R. LIVE/DEAD
pubmed: 10395466
doi: 10.1016/S0167-7012(99)00048-2
Chen Y, Zhang S, Zhai Z, Zhang S, Ma J, Liang X, et al. Construction of fusion protein with carbohydrate-binding module and leaf-branch compost cutinase to enhance the degradation efficiency of polyethylene terephthalate. Int J Mol Sci. 2023;24:2780.
pubmed: 36769118
pmcid: 9917269
doi: 10.3390/ijms24032780
Zeng W, Li X, Yang Y, Min J, Huang J-W, Liu W, et al. Substrate-binding mode of a thermophilic PET Hydrolase and engineering the enzyme to enhance the hydrolytic efficacy. ACS Catal. 2022;12:3033–40.
doi: 10.1021/acscatal.1c05800
Brizendine RK, Erickson E, Haugen SJ, Ramirez KJ, Miscall J, Salvachúa D, et al. Particle size reduction of Poly(ethylene terephthalate) increases the rate of enzymatic depolymerization but does not increase the overall conversion extent. ACS Sustain Chem Eng. 2022;10:9131–40.
doi: 10.1021/acssuschemeng.2c01961
Ho CW, Chew TK, Ling TC, Kamaruddin S, Tan WS, Tey BT. Efficient mechanical cell disruption of Escherichia coli by an ultrasonicator and recovery of intracellular hepatitis B core antigen. Process Biochem. 2006;41:1829–34.
doi: 10.1016/j.procbio.2006.03.043
Shehadul Islam M, Aryasomayajula A, Selvaganapathy P. A review on macroscale and microscale cell lysis methods. Micromachines. 2017;8:83.
pmcid: 6190294
doi: 10.3390/mi8030083
Ren X, Yu D, Han S, Feng Y. Thermolysis of recombinant Escherichia coli for recovering a thermostable enzyme. Biochem Eng J. 2007;33:94–8.
doi: 10.1016/j.bej.2006.09.017
Karayannidis GP, Chatziavgoustis AP, Achilias DS. Poly(ethylene terephthalate) recycling and recovery of pure terephthalic acid by alkaline hydrolysis. Adv Polym Technol. 2002;21:250–9.
doi: 10.1002/adv.10029
Hemmerich J, Labib M, Steffens C, Reich SJ, Weiske M, Baumgart M, et al. Screening of a genome-reduced Corynebacterium glutamicum strain library for improved heterologous cutinase secretion. Microb Biotechnol. 2020;13:2020–31.
pubmed: 32893457
pmcid: 7533341
doi: 10.1111/1751-7915.13660
Hemmerich J, Moch M, Jurischka S, Wiechert W, Freudl R, Oldiges M. Combinatorial impact of Sec signal peptides from Bacillus subtilis and bioprocess conditions on heterologous cutinase secretion by Corynebacterium glutamicum. Biotechnol Bioeng. 2019;116:644–55.
pubmed: 30450544
doi: 10.1002/bit.26873
Bakkes PJ, Ramp P, Bida A, Dohmen-Olma D, Bott M, Freudl R. Improved pEKEx2-derived expression vectors for tightly controlled production of recombinant proteins in Corynebacterium glutamicum. Plasmid. 2020;112:102540.
pubmed: 32991924
doi: 10.1016/j.plasmid.2020.102540
Silhavy TJ, Kahne D, Walker S. The bacterial cell envelope. Cold Spring Harb Perspect Biol. 2010;2:a000414–a000414.
pubmed: 20452953
pmcid: 2857177
doi: 10.1101/cshperspect.a000414
Park M, Yoo G, Bong J-H, Jose J, Kang M-J, Pyun J-C. Isolation and characterization of the outer membrane of Escherichia coli with autodisplayed Z-domains. Biochim Biophys Acta (BBA) Biomembranes. 2015;1848:842–7.
pubmed: 25528472
doi: 10.1016/j.bbamem.2014.12.011
Demchick P, Koch AL. The permeability of the wall fabric of Escherichia coli and Bacillus subtilis. J Bacteriol. 1996;178:768–73.
pubmed: 8550511
pmcid: 177723
doi: 10.1128/jb.178.3.768-773.1996
Nikaido H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev. 2003;67:593–656.
pubmed: 14665678
pmcid: 309051
doi: 10.1128/MMBR.67.4.593-656.2003
Bartesaghi A, Matthies D, Banerjee S, Merk A, Subramaniam S. Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy. Proc Natl Acad Sci. 2014;111:11709–14.
pubmed: 25071206
pmcid: 4136629
doi: 10.1073/pnas.1402809111
Sulaiman S, You D-J, Kanaya E, Koga Y, Kanaya S. Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase. Biochemistry. 2014;53:1858–69.
pubmed: 24593046
doi: 10.1021/bi401561p
Terpe K. Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol. 2006;72:211–22.
pubmed: 16791589
doi: 10.1007/s00253-006-0465-8
Jurischka S, Bida A, Dohmen-Olma D, Kleine B, Potzkei J, Binder S, et al. A secretion biosensor for monitoring Sec-dependent protein export in Corynebacterium glutamicum. Microb Cell Fact. 2020;19:11.
pubmed: 31964372
pmcid: 6975037
doi: 10.1186/s12934-019-1273-z
da Ferreira RG, Azzoni AR, Freitas S. Techno-economic analysis of the industrial production of a low-cost enzyme using E. coli: the case of recombinant β-glucosidase. Biotechnol Biofuels. 2018;11:81.
pubmed: 29610578
pmcid: 5875018
doi: 10.1186/s13068-018-1077-0
Kittler S, Kopp J, Veelenturf PG, Spadiut O, Delvigne F, Herwig C, et al. The lazarus Escherichia coli effect: recovery of productivity on glycerol/lactose mixed feed in continuous biomanufacturing. Front Bioeng Biotechnol. 2020. https://doi.org/10.3389/fbioe.2020.00993 .
doi: 10.3389/fbioe.2020.00993
pubmed: 33240864
pmcid: 7683717
Blommel PG, Becker KJ, Duvnjak P, Fox BG. Enhanced bacterial protein expression during auto-induction obtained by alteration of lac repressor dosage and medium composition. Biotechnol Prog. 2008;23:585–98.
doi: 10.1021/bp070011x
Kopp J, Kittler S, Slouka C, Herwig C, Spadiut O, Wurm DJ. Repetitive fed-batch: a promising process mode for biomanufacturing with E. coli. Front Bioeng Biotechnol. 2020. https://doi.org/10.3389/fbioe.2020.573607 .
doi: 10.3389/fbioe.2020.573607
pubmed: 33240864
pmcid: 7683717
Rosano GL, Ceccarelli EA. Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol. 2014. https://doi.org/10.3389/fmicb.2014.00172 .
doi: 10.3389/fmicb.2014.00172
pubmed: 25071752
pmcid: 4085539
Los DA, Murata N. Membrane fluidity and its roles in the perception of environmental signals. Biochim Biophys Acta BBA Biomembranes. 2004;1666:142–57.
pubmed: 15519313
doi: 10.1016/j.bbamem.2004.08.002
Ginez LD, Osorio A, Vázquez-Ramírez R, Arenas T, Mendoza L, Camarena L, et al. Changes in fluidity of the E. coli outer membrane in response to temperature, divalent cations and polymyxin-B show two different mechanisms of membrane fluidity adaptation. FEBS J. 2022;289:3550–67.
pubmed: 35038363
doi: 10.1111/febs.16358
Sührer I, Langemann T, Lubitz W, Weuster-Botz D, Castiglione K. A novel one-step expression and immobilization method for the production of biocatalytic preparations. Microb Cell Fact. 2015;14:180.
pubmed: 26577293
pmcid: 4650107
doi: 10.1186/s12934-015-0371-9
Murby M, Uhlén M, Ståhl S. Upstream strategies to minimize proteolytic degradation upon recombinant production in Escherichia coli. Protein Expr Purif. 1996;7:129–36.
pubmed: 8812844
doi: 10.1006/prep.1996.0018
Enfors S-O. Control of in vivo proteolysis in the production of recombinant proteins. Trends Biotechnol. 1992;10:310–5.
pubmed: 1369412
doi: 10.1016/0167-7799(92)90256-U
Gaur R, Lata, Khare SK. Immobilization of Xylan-degrading enzymes from Scytalidium thermophilum on Eudragit L-100. World J Microbiol Biotechnol. 2005;21:1123–8.
doi: 10.1007/s11274-005-0080-3
Bhattacharya A, Pletschke BI. Magnetic cross-linked enzyme aggregates (CLEAs): a novel concept towards carrier free immobilization of lignocellulolytic enzymes. Enzyme Microb Technol. 2014;61–62:17–27.
pubmed: 24910332
doi: 10.1016/j.enzmictec.2014.04.009
Vahidi AK, Yang Y, Ngo TPN, Li Z. Simple and efficient immobilization of extracellular his-tagged enzyme directly from cell culture supernatant as active and recyclable nanobiocatalyst: high-performance production of biodiesel from waste grease. ACS Catal. 2015;5:3157–61.
doi: 10.1021/acscatal.5b00550
Makryniotis K, Nikolaivits E, Gkountela C, Vouyiouka S, Topakas E. Discovery of a polyesterase from Deinococcus maricopensis and comparison to the benchmark LCCICCG suggests high potential for semi-crystalline post-consumer PET degradation. J Hazard Mater. 2023;455:131574.
pubmed: 37150100
doi: 10.1016/j.jhazmat.2023.131574
Geciova J, Bury D, Jelen P. Methods for disruption of microbial cells for potential use in the dairy industry—a review. Int Dairy J. 2002;12:541–53.
doi: 10.1016/S0958-6946(02)00038-9
Ho CW, Tan WS, Yap WB, Ling TC, Tey BT. Comparative evaluation of different cell disruption methods for the release of recombinant hepatitis B core antigen from Escherichia coli. Biotechnol Bioprocess Eng. 2008;13:577–83.
doi: 10.1007/s12257-008-0020-9
Pourhassan NZ, Smits SHJ, Ahn JH, Schmitt L. Biotechnological applications of type 1 secretion systems. Biotechnol Adv. 2021;53:107864.
doi: 10.1016/j.biotechadv.2021.107864
Zhou Y, Lu Z, Wang X, Selvaraj JN, Zhang G. Genetic engineering modification and fermentation optimization for extracellular production of recombinant proteins using Escherichia coli. Appl Microbiol Biotechnol. 2018;102:1545–56.
pubmed: 29270732
doi: 10.1007/s00253-017-8700-z
Rozkov A, Enfors S-O. Analysis and control of proteolysis of recombinant proteins in Escherichia coli. Berlin: Springer, Berlin Heidelberg; 2004. p. 163–95.
Kaabel S, Arciszewski J, Borchers TH, Therien JPD, Friščić T, Auclair K. Solid-state enzymatic hydrolysis of mixed PET/cotton textiles**. Chemsuschem. 2023. https://doi.org/10.1002/cssc.202201613 .
doi: 10.1002/cssc.202201613
pubmed: 36165763
Cho Y-H, Song JY, Kim KM, Kim MK, Lee IY, Kim SB, et al. Production of nattokinase by batch and fed-batch culture of Bacillus subtilis. N Biotechnol. 2010;27:341–6.
pubmed: 20541632
doi: 10.1016/j.nbt.2010.06.003
Gugel I, Vahidinasab M, Benatto Perino EH, Hiller E, Marchetti F, Costa S, et al. Fed-batch bioreactor cultivation of bacillus subtilis using vegetable juice as an alternative carbon source for lipopeptides production: a shift towards a circular bioeconomy. Fermentation. 2024;10:323.
doi: 10.3390/fermentation10060323
Ÿztürk S, Ÿalık P, Ÿzdamar TH. Fed-batch biomolecule production by bacillus subtilis: a state of the art review. Trends Biotechnol. 2016;34:329–45.
pubmed: 26775901
doi: 10.1016/j.tibtech.2015.12.008
Li P, Anumanthan A, Gao X-G, Ilangovan K, Suzara VV, Düzgüneş N, et al. Expression of recombinant proteins in Pichia Pastoris. Appl Biochem Biotechnol. 2007;142:105–24.
pubmed: 18025573
doi: 10.1007/s12010-007-0003-x
Lee J, Lee SY, Park S, Middelberg APJ. Control of fed-batch fermentations. Biotechnol Adv. 1999;17:29–48.
pubmed: 14538142
doi: 10.1016/S0734-9750(98)00015-9
Krause M, Neubauer A, Neubauer P. The fed-batch principle for the molecular biology lab: controlled nutrient diets in ready-made media improve production of recombinant proteins in Escherichia coli. Microb Cell Fact. 2016;15:110.
pubmed: 27317421
pmcid: 4912726
doi: 10.1186/s12934-016-0513-8