Research Progress on Recombinant Protein Production in the Yarrowia lipolytica Cell Factory

doi:10.19586/j.2095-2341.2026.0088

Current Biotechnology ›› 2026, Vol. 16 ›› Issue (3): 562-573.DOI: 10.19586/j.2095-2341.2026.0088

• Special Forum on Microbial Cell Factory • Previous Articles Next Articles

Research Progress on Recombinant Protein Production in the Yarrowia lipolytica Cell Factory

Xuan ZHAO¹(), Zhongxue LIU¹(), Lingling WU¹, Yongming GOU¹, Yingjie LIU²(), Wenjian MA¹()

^1.School of Bioengineering，Tianjin University of Science Technology，Tianjin 300457，China
^2.College of Biological and Chemical Engineering，Qilu Institute of Technology，Shandong Jinan 250200，China

Received:2026-04-03 Accepted:2026-05-19 Online:2026-05-25 Published:2026-07-14
Contact: Yingjie LIU,Wenjian MA

Abstract

Abstract:

High-yield recombinant protein production represents a core demand in biomanufacturing， driving the urgent need to develop genetically stable and highly productive cell factories. As a non-conventional yeast， Yarrowia lipolytica has emerged as a novel and efficient expression host due to its excellent protein secretion capacity， well-established eukaryotic post-translational modification machinery， broad substrate utilization， and favorable industrial fermentation characteristics. However， native yeast systems still face numerous challenges and often fall short of meeting the diverse requirements for recombinant protein production. The review summarized the research progress on recombinant protein production using Y. lipolytica cell factories， analyzed the characteristics of Y. lipolytica compared to common expression hosts， sorted out the core elements of its expression systems and corresponding optimization strategies， elaborated the genetic editing tools available for this host， outlined strategies and application examples for optimizing protein secretion and stability and finally， provides perspectives on future development directions， with the aim of advancing the engineering of efficient protein expression hosts.

Key words: Yarrowia lipolytica, recombinant protein, cell factory, genetic editing tools, secretion pathway

CLC Number:

Q291

Xuan ZHAO, Zhongxue LIU, Lingling WU, Yongming GOU, Yingjie LIU, Wenjian MA. Research Progress on Recombinant Protein Production in the Yarrowia lipolytica Cell Factory[J]. Current Biotechnology, 2026, 16(3): 562-573.

Add to citation manager EndNote|Ris|BibTeX

URL: https://swjsjz.magtechjournal.com/EN/10.19586/j.2095-2341.2026.0088

https://swjsjz.magtechjournal.com/EN/Y2026/V16/I3/562

Figures/Tables 4

References 80

[1]	TRIPATHI N K, SHRIVASTAVA A. Recent developments in bioprocessing of recombinant proteins: expression hosts and process development[J/OL]. Front. Bioeng. Biotechnol., 2019, 7: 420[2026-02-24]. .
[2]	TSUDA M, NAKATANI Y, BABA S, et al.. Selection of the methylotrophic yeast Ogataea minuta as a high-producing host for heterologous protein expression[J]. J. Biosci. Bioeng., 2023, 135(3): 196-202.
[3]	HU M, GE J, JIANG Y, et al.. Advances and perspectives in genetic expression and operation for the oleaginous yeast Yarrowia lipolytica [J]. Synth. Syst. Biotechnol., 2024, 9(4): 618-626.
[4]	SAWATZKI A, HANS S, NARAYANAN H, et al.. Accelerated bioprocess development of endopolygalacturonase-production with Saccharomyces cerevisiae using multivariate prediction in a 48 mini-bioreactor automated platform[J/OL]. Bioengineering, 2018, 5(4): 101[2026-03-26]. .
[5]	ANCÍN M, SANZ-BARRIO R, SANTAMARÍA E, et al.. Functional improvement of human cardiotrophin 1 produced in tobacco chloroplasts by co-expression with plastid thioredoxin m[J/OL]. Plants, 2020, 9(2): 183[2026-03-26]. .
[6]	VANDERMIES M, FICKERS P. Bioreactor-scale strategies for the production of recombinant protein in the yeast Yarrowia lipolytica [J/OL]. Microorganisms, 2019, 7(2): 40[2026-03-26]. .
[7]	YU S, ZHANG G, LIU Q, et al.. Construction and testing of Yarrowia lipolytica recombinant protein expression chassis cells based on the high-throughput screening and secretome[J/OL]. Microb. Cell Fact., 2023, 22(1): 185[2026-03-26]. .
[8]	MCKENZIE E A, ABBOTT W M. Expression of recombinant proteins in insect and mammalian cells[J]. Methods, 2018, 147: 40-49.
[9]	JAZAYERI S H, AMIRI-YEKTA A, BAHRAMI S, et al.. Vector and cell line engineering technologies toward recombinant protein expression in mammalian cell lines[J]. Appl. Biochem. Biotechnol., 2018, 185(4): 986-1003.
[10]	ZAHN-ZABAL M, KOBR M, GIROD P A, et al.. Development of stable cell lines for production or regulated expression using matrix attachment regions[J]. J. Biotechnol., 2001, 87(1): 29-42.
[11]	SHANMUGARAJ B, MALLA A, PHOOLCHAROEN W. Emergence of novel coronavirus 2019-nCoV: need for rapid vaccine and biologics development[J/OL]. Pathogens, 2020, 9(2): 148[2026-03-26]. .
[12]	POURESMAEIL M, AZIZI-DARGAHLOU S. Factors involved in heterologous expression of proteins in E . coli host[J/OL]. Arch. Microbiol., 2023, 205(5): 212[2026-03-26]. .
[13]	LIU L, QIAO B, RONG J, et al.. The removal of endotoxins in the actual production process[J]. Int. J. Public Health Med. Res., 2024, 2(1): 165-172.
[14]	MOHAMMADZADEH R, KARBALAEI M, SOLEIMANPOUR S, et al.. Practical methods for expression of recombinant protein in the Pichia pastoris system[J/OL]. Curr. Protoc., 2021, 1(6): e155[2026-03-26]. .
[15]	VIEIRA GOMES A M, CARMO T S, CARVALHO L S, et al.. Comparison of yeasts as hosts for recombinant protein production[J/OL]. Microorganisms, 2018, 6(2): 38[2026-03-26]. .
[16]	FRIEDMAN B, VADDI K, PRESTON C, et al.. A comparison of the pharmacological properties of carbohydrate remodeled recombinant and placental-derived β-glucocerebrosidase: implications for clinical efficacy in treatment of Gaucher disease[J]. Blood, 1999, 93(9): 2807-2816.
[17]	TSUDA M, NONAKA K. Recent progress on heterologous protein production in methylotrophic yeast systems[J/OL]. World J. Microbiol. Biotechnol., 2024, 40(7): 200[2026-03-26]. .
[18]	INNIS M A, HOLLAND M J, MCCABE P C, et al.. Expression, glycosylation, and secretion of an Aspergillus glucoamylase by Saccharomyces cerevisiae [J]. Science, 1985, 228(4695): 21-26.
[19]	HEIMO H, PALMU K, SUOMINEN I. Expression in Pichia pastorisand purification of Aspergillus awamori glucoamylase catalytic domain[J]. Protein Expr. Purif., 1997, 10(1): 70-79.
[20]	KIM K, CHOE D, LEE D H, et al.. Engineering biology to construct microbial chassis for the production of difficult-to-express proteins[J/OL]. Int. J. Mol. Sci., 2020, 21(3): 990[2026-03-26]. .
[21]	LIU C, GONG J S, SU C, et al.. Pathway engineering facilitates efficient protein expression in Pichia pastoris [J]. Appl. Microbiol. Biotechnol., 2022, 106(18): 5893-5912.
[22]	WANG W, BLENNER M A. Engineering heterologous enzyme secretion in Yarrowia lipolytica [J/OL]. Microb. Cell Fact., 2022, 21(1): 134[2026-03-26]. .
[23]	NICAUD J M, MADZAK C, VAN DEN BROEK P, et al.. Protein expression and secretion in the yeast Yarrowia lipolytica [J]. FEMS Yeast Res., 2002, 2(3): 371-379.
[24]	LI X, YE C, LIU T, et al.. Engineering genetic elements for microbial protein expression systems: advances, challenges, applications, and prospects[J]. Synth. Syst. Biotechnol., 2026, 11: 370-384.
[25]	MADZAK C. Yarrowia lipolytica: recent achievements in heterologous protein expression and pathway engineering[J]. Appl. Microbiol. Biotechnol., 2015, 99(11): 4559-4577.
[26]	WANG W, WEI H, ALAHUHTA M, et al.. Heterologous expression of xylanase enzymes in lipogenic yeast Yarrowia lipolytica [J/OL]. PLoS One, 2014, 9(12): e111443[2026-03-26]. .
[27]	NARS G, SAUREL O, BORDES F, et al.. Production of stable isotope labelled lipase Lip2 from Yarrowia lipolytica for NMR: investigation of several expression systems[J]. Protein Expr. Purif., 2014, 101: 14-20.
[28]	WU Z, CHEN W, HONG Y, et al.. Machine learning-assisted rational design and evolution of novel signal peptides in Yarrowia lipolytica [J]. Synth. Syst. Biotechnol., 2025, 10(4): 1275-1283.
[29]	SPAGNUOLO M, SHABBIR HUSSAIN M, GAMBILL L, et al.. Alternative substrate metabolism in Yarrowia lipolytica [J/OL]. Front. Microbiol., 2018, 9: 1077[2026-03-26]. .
[30]	KATRE G, AJMERA N, ZINJARDE S, et al.. Mutants of Yarrowia lipolytica NCIM 3589 grown on waste cooking oil as a biofactory for biodiesel production[J/OL]. Microb. Cell Fact., 2017, 16(1): 176[2026-03-26]. .
[31]	SWENNEN D, BECKERICH J M. Yarrowia lipolytica vesicle-mediated protein transport pathways[J/OL]. BMC Evol. Biol., 2007, 7(1): 219[2026-03-26]. .
[32]	LIU X, DENG J, ZHANG J, et al.. Genome-scale transcriptional activation by non-homologous end joining-mediated integration in Yarrowia lipolytica [J/OL]. Biotechnol. Biofuels Bioprod., 2024, 17(1): 24[2026-03-26]. .
[33]	LARROUDE M, ROSSIGNOL T, NICAUD J M, et al.. Synthetic biology tools for engineering Yarrowia lipolytica [J]. Biotechnol. Adv., 2018, 36(8): 2150-2164.
[34]	ONÉSIME D, LEBRUN E, PETROVIC G S, et al.. New Yarrowia lipolytica chassis strains for industrial enzyme production[J/OL]. Microb. Cell Fact., 2025, 24(1): 164[2026-03-26]. .
[35]	WU Y, LI S, SUN B, et al.. Enhancing gastrodin production in Yarrowia lipolytica by metabolic engineering[J]. ACS Synth. Biol., 2024, 13(4): 1332-1342.
[36]	DIAS B, LOPES M, FERNANDES H, et al.. Biomass and microbial lipids production by Yarrowia lipolytica W29 from Eucalyptus bark hydrolysate[J/OL]. Renew. Energy, 2024, 224: 120173[2026-03-26]. .
[37]	MADZAK C. Yarrowia lipolytica strains and their biotechnological applications: how natural biodiversity and metabolic engineering could contribute to cell factories improvement[J/OL]. J. Fungi, 2021, 7(7): 548[2026-03-26]. .
[38]	DE POURCQ K, VERVECKEN W, DEWERTE I, et al.. Engineering the yeast Yarrowia lipolytica for the production of therapeutic proteins homogeneously glycosylated with Man8GlcNAc2 and Man5GlcNAc2[J/OL]. Microb. Cell Fact., 2012, 11(1): 53[2026-03-26]. .
[39]	MAMAEV D, ZVYAGILSKAYA R. Yarrowia lipolytica: a multitalented yeast species of ecological significance[J/OL]. FEMS Yeast Res., 2021, 21(2): foab008[2026-03-26]. .
[40]	MÜLLER S, SANDAL T, KAMP-HANSEN P, et al.. Comparison of expression systems in the yeasts Saccharomyces cerevisiae, Hansenula polymorpha, Klyveromyces lactis, Schizosaccharomyces pombe and Yarrowia lipolytica. Cloning of two novel promoters from Yarrowia lipolytica [J]. Yeast, 1998, 14(14): 1267-1283.
[41]	SASSI H, DELVIGNE F, KAR T, et al.. Deciphering how LIP2 and POX2 promoters can optimally regulate recombinant protein production in the yeast Yarrowia lipolytica [J/OL]. Microb. Cell Fact., 2016, 15(1): 159[2026-03-26]. .
[42]	DULERMO R, BRUNEL F, DULERMO T, et al.. Using a vector pool containing variable-strength promoters to optimize protein production in Yarrowia lipolytica [J/OL]. Microb. Cell Fact., 2017, 16: 31[2026-03-26]. .
[43]	STROUD R M, WALTER P. Signal sequence recognition and protein targeting[J]. Curr. Opin. Struct. Biol., 1999, 9(6): 754-759.
[44]	RAPIEJKO P J, GILMORE R. Empty site forms of the SRP54 and SRα GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum[J]. Cell, 1997, 89(5): 703-713.
[45]	CURRAN K A, MORSE N J, MARKHAM K A, et al.. Short synthetic terminators for improved heterologous gene expression in yeast[J]. ACS Synth. Biol., 2015, 4(7): 824-832.
[46]	MADZAK C, BECKERICH J M. Heterologous protein expression and secretion in Yarrowia lipolytica [M]// Yarrowia lipolytica. Heidelberg: Springer, 2013: 1-76.
[47]	朱星宇.基于分泌途径工程改造解脂耶氏酵母高效合成Monellin的研究[D].无锡:江南大学,2025.
[48]	WANG B, ZHOU X, WANG Y, et al.. Enhancement of thermostability and expression level of Rasamsonia emersonii lipase in Pichia pastoris and its application in biodiesel production in a continuous flow reactor[J/OL]. Int. J. Biol. Macromol., 2024, 278: 134481[2026-03-26]. .
[49]	LEDER A, MAS G, SZENTGYÖRGYI V, et al.. A multichaperone condensate enhances protein folding in the endoplasmic reticulum[J]. Nat. Cell Biol., 2025, 27(9): 1422-1430.
[50]	MAYER M P, GIERASCH L M. Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones[J]. J. Biol. Chem., 2019, 294(6): 2085-2097.
[51]	HONG S P, SEIP J, WALTERS-POLLAK D, et al.. Engineering Yarrowia lipolytica to express secretory invertase with strong FBA1IN promoter[J]. Yeast, 2012, 29(2): 59-72.
[52]	AN J, ZHANG L, LI L, et al... An alternative approach to synthesizing galactooligosaccharides by cell-surface display of β-galactosidase on Yarrowia lipolytica [J]. J. Agric. Food Chem., 2016, 64(19): 3819-3827.
[53]	PARK Y K, VANDERMIES M, SOUDIER P, et al.. Efficient expression vectors and host strain for the production of recombinant proteins by Yarrowia lipolytica in process conditions[J/OL]. Microb. Cell Fact., 2019, 18(1): 167[2026-03-26]. .
[54]	LUKITO B R, SOFEO N, LIM H J, et al.. Expanding biotechnological applications of Yarrowia lipolytica: key advances in the past decade[J/OL]. Biotechnol. Adv., 2026, 88: 108835[2026-03-26]. .
[55]	CURRAN K A, KARIM A S, GUPTA A, et al.. Use of expression-enhancing terminators in Saccharomyces cerevisiae to increase mRNA half-life and improve gene expression control for metabolic engineering applications[J]. Metab. Eng., 2013, 19: 88-97.
[56]	CHEN Q H, QIAN Y D, NIU Y J, et al.. Characterization of an efficient CRISPR-iCas9 system in Yarrowia lipolytica for the biosynthesis of carotenoids[J]. Appl. Microbiol. Biotechnol., 2023, 107(20): 6299-6313.
[57]	LIU J, ZHU Y, HOU J. Optimizing the CRISPR/Cas9 system for gene editing in Yarrowia lipolytica [J/OL]. Eng. Microbiol., 2025, 5(2): 100193[2026-03-26]. .
[58]	JONSDOTTIR T, PAOLETTA M, HENRIKSSON J, et al.. Plasmodium berghei high-throughput (PbHiT): a CRISPR-Cas9 system to study genes at scale[J/OL]. Bio Protoc., 2026, 16(2): e5572[2026-03-26]. .
[59]	VERBEKE J, BEOPOULOS A, NICAUD J M. Efficient homologous recombination with short length flanking fragments in Ku70 deficient Yarrowia lipolytica strains[J]. Biotechnol. Lett., 2013, 35(4): 571-576.
[60]	MADZAK C, TRÉTON B, BLANCHIN-ROLAND S. Strong hybrid promoters and integrative expression/secretion vectors for quasi-constitutive expression of heterologous proteins in the yeast Yarrowia lipolytica [J]. J. Mol. Microbiol. Biotechnol., 2000, 2(2): 207-216.
[61]	LAZAR Z, ROSSIGNOL T, VERBEKE J, et al.. Optimized invertase expression and secretion cassette for improving Yarrowia lipolytica growth on sucrose for industrial applications[J]. J. Ind. Microbiol. Biotechnol., 2013, 40(11): 1273-1283.
[62]	LIU M, ZHANG J, LIU X, et al.. Rapid gene target tracking for enhancing β-carotene production using flow cytometry-based high-throughput screening in Yarrowia lipolytica [J]. Appl. Environ. Microbiol., 2022, 88(19): 1122-1149.
[63]	RAMESH A, TRIVEDI V, LEE S, et al.. acCRISPR: an activity-correction method for improving the accuracy of CRISPR screens[J/OL]. Commun. Biol., 2023, 6: 617[2026-03-26]. .
[64]	HENKEL L, RAUSCHER B, SCHMITT B, et al.. Genome-scale CRISPR screening at high sensitivity with an empirically designed sgRNA library[J/OL]. BMC Biol., 2020, 18: 174[2026-03-26]. .
[65]	ZHU X, LI M, ZHU R, et al.. Up front unfolded protein response combined with early protein secretion pathway engineering in Yarrowia lipolytica to attenuate ER stress caused by enzyme overproduction[J/OL]. Int. J. Mol. Sci., 2023, 24(22): 16426[2026-03-26]. .
[66]	VIDAL L, DONG Z, OLOFSSON K, et al.. Production of Rhizopus oryzae lipase using optimized Yarrowia lipolytica expression system[J/OL]. FEMS Yeast Res., 2023, 23: foad037[2026-03-26]. .
[67]	DAI X P, MENG X C, ZHOU Y J, et al.. De Novo design of high-performance sec-type signal peptide via a hybrid deep learning architecture[J]. JACS Au, 2025, 5(10): 4669-4674.
[68]	JIAO L, LI W, LI Y, et al.. Employing engineered enolase promoter for efficient expression of Thermomyces lanuginosus lipase in Yarrowia lipolytica via a self-excisable vector[J/OL]. Int. J. Mol. Sci., 2023, 24(1): 719[2026-03-26]. .
[69]	KORPYS-WOŹNIAK P, KUBIAK P, CELIŃSKA E. Secretory helpers for enhanced production of heterologous proteins in Yarrowia lipolytica [J/OL]. Biotechnol. Rep., 2021, 32: e00669[2026-03-26]. .
[70]	MADZAK C, GAILLARDIN C, BECKERICH J M. Heterologous protein expression and secretion in the non-conventional yeast Yarrowia lipolytica: a review[J]. J. Biotechnol., 2004, 109(1-2): 63-81.
[71]	TRASSAERT M, VANDERMIES M, CARLY F, et al.. New inducible promoter for gene expression and synthetic biology in Yarrowia lipolytica [J/OL]. Microb. Cell Fact., 2017, 16(1): 141[2026-03-26]. .
[72]	SWIETALSKI P, HETZEL F, SEITL I, et al.. Secretion of a low and high molecular weight β-glycosidase by Yarrowia lipolytica [J/OL]. Microb. Cell Fact., 2020, 19: 100[2026-03-26]. .
[73]	ROBINSON A S, HINES V, WITTRUP K D. Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae [J]. Technology, 1994, 12(4): 381-384.
[74]	DARVISHI F, MORADI M, JOLIVALT C, et al.. Laccase production from sucrose by recombinant Yarrowia lipolytica and its application to decolorization of environmental pollutant dyes[J]. Ecotoxicol. Environ. Saf., 2018, 165: 278-283.
[75]	YANG S, SHEN J, DENG J, et al.. Engineering cell polarization improves protein production in Saccharomyces cerevisiae [J/OL]. Microorganisms, 2022, 10(10): 2005[2026-03-26]. .
[76]	OUEPHANIT C, BOONVITTHYA N, THEERACHAT M, et al.. Efficient expression and secretion of endo-1, 4-β-xylanase from Penicillium citrinum in non-conventional yeast Yarrowia lipolytica directed by the native and the preproLIP2 signal peptides[J]. Protein Expr. Purif., 2019, 160: 1-6.
[77]	KHADIVI DERAKSHAN F, DARVISHI F, DEZFULIAN M, et al.. Expression and characterization of glucose oxidase from Aspergillus niger in Yarrowia lipolytica [J]. Mol. Biotechnol., 2017, 59(8): 307-314.
[78]	MIRANDA S M, BELO I, LOPES M. Yarrowia lipolytica growth, lipids, and protease production in medium with higher alkanes and alkenes[J/OL]. World J. Microbiol. Biotechnol., 2024, 40(10): 318[2026-03-26]. .
[79]	陈云.植酸酶phyA基因在解脂耶氏酵母中的表达研究[D].成都:四川师范大学,2010.
[80]	DE POURCQ K, TIELS P, VAN HECKE A, et al.. Engineering Yarrowia lipolytica to produce glycoproteins homogeneously modified with the universal Man3GlcNAc2 N-glycan core[J/OL]. PLoS One, 2012, 7(6): e39976[2026-03-26]. .

菌株	基因型	特征	参考文献
W29（CLIB89）	WT	MatA法国野生型菌株、基因组已经被测序	[23]
E129	lys11-23、leu2-270、ura3-302、xpr2-322	MatA、含有zeta序列元件的菌株	[40]
E150	his1、leu2-270、ura3-302、xpr2-322	MatB、含有zeta序列元件的菌株、参考菌株、基因组已经被测序	[41]
H222（CLIB80）	WT	MatA德国野生型菌株，擅长利用烷烃，常用于油脂生产相关研究	[23]
Po1d（CLIB139）	leu2-270、ura3-302、xpr2-322、Leu^-、Ura^-、ΔAEP、Suc⁺	MatA、不含zeta序列元件的菌株	[42]
Po1e（CLIB723）	leu2-270、ura3-302::URA3、xpr2-322、Leu^-、ΔAEP、Suc⁺	MatA、基于pBR322的整合平台	[43]
Po1f（CLIB724）	leu2-270、ura3-302、xpr2-322、axp1-2、Leu^-、Ura^-、ΔAEP、ΔAXP、Suc⁺	MatA、应用最广的工业底盘，去除了主要胞外蛋白酶（XPR2），有利于异源蛋白表达	[43]
Po1g（CLIB725）	leu2-270、ura3-302::URA3、xpr2-322、axp1-2Leu^-、ΔAEP、ΔAXP、Suc⁺	MatA、基于pBR322的整合平台，与Po1f相似，但保留了蛋白酶活性，适用于不同实验需求	[43]
Po1h（CLIB882）	ura3-302、xpr2-322、axp1-2、Ura^-、ΔAEP、ΔAXP、Suc⁺	MatA、单营养缺陷型，适合只需要单个筛选标记的场景	[44]
Y1212	leu2-270、ura3-302、xpr2-322、Leu^-、Ura^-、ΔLIP2、ΔLIP7、ΔLIP8	MatA、含有zeta序列元件的菌株	[44]

菌株	基因型	特征	参考文献
W29（CLIB89）	WT	MatA法国野生型菌株、基因组已经被测序	[23]
E129	lys11-23、leu2-270、ura3-302、xpr2-322	MatA、含有zeta序列元件的菌株	[40]
E150	his1、leu2-270、ura3-302、xpr2-322	MatB、含有zeta序列元件的菌株、参考菌株、基因组已经被测序	[41]
H222（CLIB80）	WT	MatA德国野生型菌株，擅长利用烷烃，常用于油脂生产相关研究	[23]
Po1d（CLIB139）	leu2-270、ura3-302、xpr2-322、Leu^-、Ura^-、ΔAEP、Suc⁺	MatA、不含zeta序列元件的菌株	[42]
Po1e（CLIB723）	leu2-270、ura3-302::URA3、xpr2-322、Leu^-、ΔAEP、Suc⁺	MatA、基于pBR322的整合平台	[43]
Po1f（CLIB724）	leu2-270、ura3-302、xpr2-322、axp1-2、Leu^-、Ura^-、ΔAEP、ΔAXP、Suc⁺	MatA、应用最广的工业底盘，去除了主要胞外蛋白酶（XPR2），有利于异源蛋白表达	[43]
Po1g（CLIB725）	leu2-270、ura3-302::URA3、xpr2-322、axp1-2Leu^-、ΔAEP、ΔAXP、Suc⁺	MatA、基于pBR322的整合平台，与Po1f相似，但保留了蛋白酶活性，适用于不同实验需求	[43]
Po1h（CLIB882）	ura3-302、xpr2-322、axp1-2、Ura^-、ΔAEP、ΔAXP、Suc⁺	MatA、单营养缺陷型，适合只需要单个筛选标记的场景	[44]
Y1212	leu2-270、ura3-302、xpr2-322、Leu^-、Ura^-、ΔLIP2、ΔLIP7、ΔLIP8	MatA、含有zeta序列元件的菌株	[44]

启动子	特征	参考文献
pTEF1	内源；组成型	[43]
pTDH1	内源；组成型	[44]
pFBA1	内源；组成型	[44]
pGPD	内源；组成型	[45]
FBA1IN	杂合；组成型	[44]
pXPR2	内源；诱导型	[46]
pICL1	内源；诱导型	[45]
pPOT1	内源；诱导型	[45]
pPOX1、pPOX2、pPOX5	内源；诱导型	[45]
pLIP2	内源；烷烃、脂肪酸及其衍生物诱导型	[47]
pYAT	内源；低氮诱导型	[48]
pLEU2	内源；亮氨酸前体诱导型	[49]
pEYK1	内源；赤藓糖醇、赤藓酮糖诱导型及葡萄糖、甘油抑制型	[28]
php4d	杂合；组成型	[50]

启动子	特征	参考文献
pTEF1	内源；组成型	[43]
pTDH1	内源；组成型	[44]
pFBA1	内源；组成型	[44]
pGPD	内源；组成型	[45]
FBA1IN	杂合；组成型	[44]
pXPR2	内源；诱导型	[46]
pICL1	内源；诱导型	[45]
pPOT1	内源；诱导型	[45]
pPOX1、pPOX2、pPOX5	内源；诱导型	[45]
pLIP2	内源；烷烃、脂肪酸及其衍生物诱导型	[47]
pYAT	内源；低氮诱导型	[48]
pLEU2	内源；亮氨酸前体诱导型	[49]
pEYK1	内源；赤藓糖醇、赤藓酮糖诱导型及葡萄糖、甘油抑制型	[28]
php4d	杂合；组成型	[50]

菌株	底物	产物	产量/（U·mL^-1）	参考文献
JMY1212	甘油	脂肪酶	45 125	[73]
Po1g	蔗糖	漆酶	6 760	[74]
Po1g	甘油	α-淀粉酶	22 979.2	[75]
JMP62UraTEF	葡萄糖	木聚糖酶A	180	[76]
Po1g	葡萄糖	葡萄糖氧化酶	370	[77]
CBS 2075	混合脂肪烃	蛋白酶	3 423	[78]
Po1h	葡萄糖	植酸酶	636.23	[79]

Research Progress on Recombinant Protein Production in the Yarrowia lipolytica Cell Factory

RichHTML

PDF

Knowledge

Abstract

Cite this article

share this article

Figures/Tables 4

References 80

Related Articles 6

Recommended Articles

Metrics

Comments

[1]	Wenzhu WEI, Sen PANG, Xiaoli HUANG, Jian WANG, Xing FAN, Siyan CHEN, Yujian CHEN, Jian JIAO. Engineering Microbial Cell Factories: Advances in Material Systems and Biomanufacturing Technologies [J]. Current Biotechnology, 2026, 16(3): 574-584.
[2]	Yingjie LIU, Ying MA, Yide LI, Dongqing KONG, Hanyu LIU. Metabolic Regulation Strategies for Aromatic Amino Acids and Derivatives in Yeast: A Review [J]. Current Biotechnology, 2026, 16(3): 549-561.
[3]	Juan LI, Yuting HE, Xiaoxuan YE, Jiayi JIA, Yaohui ZHANG, Hongyang ZHANG, Tao WU. Metabolic Engineering Strategies and Application Advances of Microbial Cell Factories for Carotenoid Production [J]. Current Biotechnology, 2026, 16(3): 523-534.
[4]	Xiaoyu WANG, Lin CUI, Miao LIU, Huiying LUO, Bin YAO, Xiaolu WANG. Research Advances on the Resource Utilization of Carbon Dioxide Based on Microbial Cell Factories [J]. Current Biotechnology, 2026, 16(3): 454-484.
[5]	Zhaohui CUI, Ling GUO, Xudong SHEN, Yi LIN, Lili ZHAI. Research Progress on Yeast Expression of Therapeutic Recombinant Proteins [J]. Current Biotechnology, 2025, 15(3): 380-387.
[6]	Chunyue ZHANG, Jiayang JIN, Yongjun QIU, Liqiang FAN, Liming ZHAO. Collision Between Tradition and Future: Technology and Application Progress in Food Fermentation Engineering [J]. Current Biotechnology, 2021, 11(4): 418-429.