Current Developments on the Cloning and Expression of Microbial Phospholipase D

DONG Zixing; YANG Shuangshuang; TANG Cunduo; YAO Lunguang; KAN Yunchao

doi:10.13386/j.issn1002-0306.2020070257

Volume 42 Issue 15

Jul. 2021

Turn off MathJax

Article Contents

Abstract

References

Science and Technology of Food Industry > 2021 > 42(15): 396-402. > DOI: 10.13386/j.issn1002-0306.2020070257

DONG Zixing, YANG Shuangshuang, TANG Cunduo, et al. Current Developments on the Cloning and Expression of Microbial Phospholipase D[J]. Science and Technology of Food Industry, 2021, 42(15): 396−402. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2020070257.

Citation:

PDF (939 KB)

Current Developments on the Cloning and Expression of Microbial Phospholipase D

1.
Henan Provincial Engineering Laboratory of Insect Bio-reactor and Henan Key Laboratory of Ecological Security of Water Source Region of Mid-line of South-to-North, Nanyang Normal University, Nanyang 473061, China
2.
College of Physical Education, Nanyang Normal University, Nanyang 473061, China

More Information

Received Date: July 21, 2020
Available Online: May 30, 2021

Graphical Abstract

Abstract

Abstract

Phospholipase D (PLD, EC 3.1.4.4) is a suite of enzymes catalyzing the hydrolysis of the phosphodiester bond of phospholipids, and the transfer of phosphatidic acid to primary alcohols to generate different phospholipids. The transphosphatidylation reaction makes PLD have wide applications in food, pharmaceutical and cell biology fields. However, large-scale industrial production of PLD has been restricted by many factors. Genetic engineering technology has therefore been adopted to clone and express PLD genes to obtain PLD with high quality, high purity and high transphosphatidylation activity. In this review, current progresses on the cloning and high-efficiency expression of microbial phospholipase D are analyzed, with a hope to guide the large-scale industrial production of PLD and lay a solid foundation for the development and utilization of related products.

FullText(HTML)

References (52)

References

[1]	杨学利, 马沁沁, 袁向华, 等. 磷脂酶D及其催化机制的研究进展[J]. 中国油脂,2016,41(3):80−84. doi: 10.3969/j.issn.1003-7969.2016.03.019
[2]	Shim J K, Caron M A, Weatherly L M, et al. Antimicrobial agent triclosan suppresses mast cell signaling via phospholipase D inhibition[J]. Journal of Applied Toxicology,2019,39(12):1672−1690. doi: 10.1002/jat.3884
[3]	Cho J H, Han J S. Phospholipase D and its essential role in cancer[J]. Molecular Cells,2017,40(11):805−813.
[4]	Mao X, Liu Q, Qiu Y, et al. Identification of a novel phospholipase D with high transphosphatidylation activity and its application in synthesis of phosphatidylserine and DHA-phosphatidylserine[J]. Journal of Biotechnology,2017,249:51−58. doi: 10.1016/j.jbiotec.2017.03.029
[5]	Arranz-Martínez P, Casado V, Reglero G, et al. Novel glyceryl ethers phospholipids produced by solid to solid transphosphatidylation in the presence of a food grade phospholipase D[J]. European Journal of Lipid Science & Technology,2017,119(9):1600427.
[6]	Zhang Z, Chen M, Xu W, et al. Microbial phospholipase D: Identification, modification and application[J]. Trends in Food Science & Technology,2020,96:145−156.
[7]	Tao X Y, Jia N, Cheng N H, et al. Design and evaluation of a phospholipase D based drug delivery strategy of novel phosphatidyl-prodrug[J]. Biomaterials,2017,131:1−14. doi: 10.1016/j.biomaterials.2017.03.045
[8]	Zhou W B, Gong J S, Hou H J, et al. Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine[J]. Bioengineered,2017,9(1):80−89.
[9]	Zambonelli C, Morandi P, Vanoni M A, et al. Cloning and expression in Escherichia coli of the gene encoding Streptomyces PMF PLD, a phospholipase D with high transphosphatidylation activity[J]. Enzyme & Microbial Technology,2003,33(5):676−688.
[10]	李斌, 路福平, 史文玉, 等. 色褐链霉菌磷脂酶D基因pld的克隆与表达[J]. 化学与生物工程,2007,24(5):48−51. doi: 10.3969/j.issn.1672-5425.2007.05.016
[11]	Ogino C, Kanemasu M, Hayashi Y, et al. Over-expression system for secretory phospholipase D by Streptomyces lividans[J]. Applied Microbioliogy & Biotechnology,2004,64(6):823−828.
[12]	Kokusho Y, Kato S, Machida H, et al. Purification and properties of phospholipase D from Actinomadura sp. strain No. 362[J]. Journal of the Agricultural Chemical Society of Japan,2006,51(9):2515−2524.
[13]	Zhao Y, Xu Y, Yu F, et al. Identification of a novel phospholipase D gene and effects of carbon sources on its expression in Bacillus cereus ZY12[J]. Journal of Microbiology,2018,56(4):264−271. doi: 10.1007/s12275-018-7529-1
[14]	Songer J G, Libby S J, Iandolo J J, et al. Cloning and expression of the phospholipase D gene from Corynebacterium pseudotuberculosis in Escherichia coli[J]. Infect & Immunity,1990,58(1):131−136.
[15]	Matsumoto Y, Kashiwabara N, Oyama T, et al. Molecular cloning, heterologous expression, and enzymatic characterization of lysoplasmalogen-specific phospholipase D from Thermocrispum sp.[J]. FEBS Open Bio,2016,6(11):1113−1130. doi: 10.1002/2211-5463.12131
[16]	Tsuruta H, Hayashi R, Ohkawa H, et al. Characterisitics and gene cloning of phospholipase D of the psychrophile, Shewanella sp.[J]. Bioscience, Biotechnology and Biochemistry,2007,71(10):2534−2542. doi: 10.1271/bbb.70325
[17]	Lery L M, Frangeul L, Tomas A, et al. Comparative analysis of Klebsiella pneumoniae genomes identifies a phospholipase D family protein as a novel virulence factor[J]. BMC Biology,2014,12(1):1−15. doi: 10.1186/1741-7007-12-1
[18]	Yang L, Xu Y, Chen Y, et al. Efficient extracellular expression of phospholipase D in Escherichia coli with an optimized signal peptide[A]. IOP Conference, 2018; 301: p 012105.
[19]	Zhang Y N, Lu F P, Chen G Q, et al. Expression, purification, and characterization of phosphatidylserine synthase from Escherichia coli K₁₂ in Bacillus subtilis[J]. Journal of Agricultural and Food Chemistry,2009,57(1):122−126. doi: 10.1021/jf802664u
[20]	Cole R, Proulx P. Phospholipase D activity of gram-negative bacteria[J]. Journal of Bacteriology,1975,124(3):1148−1152. doi: 10.1128/JB.124.3.1148-1152.1975
[21]	胡飞. 磷脂酶D制备及其催化合成磷脂酰丝氨酸研究[D]. 合肥: 合肥工业大学, 2013.
[22]	Wang F, Wu Z, Abousalham A, et al. Deletion the C-terminal peptides of Vibrio harveyi phospholipase D significantly improved its enzymatic properties[J]. International Journal of Biological Macromolecules,2019,129:1140−1147. doi: 10.1016/j.ijbiomac.2018.12.097
[23]	Waksman M, Eli Y, Liscovitch M, et al. Identification and characterization of a gene encoding phospholipase D activity in yeast[J]. Journal of Biological Chemistry,1996,271(5):2361−2364. doi: 10.1074/jbc.271.5.2361
[24]	Kanoh H, Nakashima S, Zhao Y, et al. Molecular cloning of a gene encoding phospholipase D from the pathogenic and dimorphic fungus, Candida albicans[J]. Biochim Biophys Acta,1998,1398(3):359−364. doi: 10.1016/S0167-4781(98)00067-0
[25]	Harkins A L, Yuan G, London S D, et al. An oleate-stimulated, phosphatidylinositol 4, 5-bisphosphate-independent phospholipase D in Schizosaccharomyces pombe[J]. FEMS Yeast Research,2010,10(6):717−726. doi: 10.1111/j.1567-1364.2010.00646.x
[26]	Li X, Gao M, Han X, et al. Disruption of the phospholipase D gene attenuates the virulence of Aspergillus fumigatus[J]. Infect & Immunity,2012,80(1):429−440.
[27]	石创, 张薇, 王一丁. 磷脂酶D产生菌株的筛选及其转磷脂化反应特性[J]. 四川大学学报: 自然科学版,2016,53(1):215−220.
[28]	朱其立. 禾谷镰刀菌磷脂酶D基因家族功能分析[D]. 泰安: 山东农业大学, 2017.
[29]	Yang H, Roberts M F. Cloning, overexpression, and characterization of a bacterial Ca²⁺-dependent phospholipase D[J]. Protein Science,2002,11(12):2958−2968.
[30]	张忆雪. 酶法制磷脂酰丝氨酸[D]. 北京: 北京化工大学, 2013.
[31]	刘立明, 秦雯, 吴承晋, 等. 一种产磷脂酶D的重组大肠杆菌及其应用: 中国, CN107384844A [P]. 2017-11-24.
[32]	Lee J S, Bat-Ochir M, Demirev A V, et al. Molecular cloning of the phospholipase D gene from Streptomyces sp. YU100 and its expression in Escherichia coli[J]. Journal of Microbiology,2009,47(1):116−122. doi: 10.1007/s12275-008-0161-8
[33]	Hou H J, Gong J S, Dong Y X, et al. Phospholipase D engineering for improving the biocatalytic synthesis of phosphatidylserine[J]. Bioprocess and Biosystems Engineering,2019,42(7):1185−1194. doi: 10.1007/s00449-019-02116-7
[34]	Zhang H, Chu W, Sun J, et al. Combining cell surface display and DNA-shuffling technology for directed evolution of Streptomyces phospholipase D and synthesis of phosphatidylserine[J]. Journal of Agricultural and Food Chemistry,2019,67(47):13119−13126. doi: 10.1021/acs.jafc.9b05394
[35]	Liu Y, Zhang T, Qiao J, et al. High-yield phosphatidylserine production via yeast surface display of phospholipase D from Streptomyces chromofuscus on Pichia pastoris[J]. Journal of Agricultural and Food Chemistry,2014,62(23):5354−5360. doi: 10.1021/jf405836x
[36]	Iwasaki Y, Mishima N, Mizumoto K, et al. Extracellular production of phospholipase D of Streptomyces antibioticus using recombinant Escherichia coli[J]. Journal of Fermentation and Bioengineering,1995,79(5):417−421. doi: 10.1016/0922-338X(95)91254-3
[37]	Xiong W, Zeng X, Ho S H, et al. Strategies for achieving high-level and stable production of toxic Streptomyces phospholipase D in Escherichia coli[J]. Journal of Chemical Technology & Biotechnology,2019,94(4):1220−1229.
[38]	Tao X, Zhao M, Zhang Y, et al. Comparison of the expression of phospholipase D from Streptomyces halstedii in different hosts and its over-expression in Streptomyces lividans[J]. FEMS Microbiology Letters,2019,366(5):fnz051.
[39]	张莹. 在不同宿主中表达链霉菌磷脂酶D的研究[D]. 上海: 华东理工大学, 2013.
[40]	Liu Y, Huang L, Fu Y, et al. A novel process for phosphatidylserine production using a Pichia pastoris whole-cell biocatalyst with overexpression of phospholipase D from Streptomyces halstedii in a purely aqueous system[J]. Food Chemistry,2019,274:535−542. doi: 10.1016/j.foodchem.2018.08.105
[41]	黄琳, 马杰莹, 王爽, 等. Streptomyces septatus磷脂酶D在毕赤酵母中的重组表达及酶学性质分析[J]. 食品科学,2020(8):100−107. doi: 10.7506/spkx1002-6630-20190903-029
[42]	Matsumoto Y, Sugimori D. Substrate recognition mechanism of Streptomyces phospholipase D and enzymatic measurement of plasmalogen[J]. Journal of Bioscience and Bioengineering,2015,120(4):372−379. doi: 10.1016/j.jbiosc.2015.02.020
[43]	Nakazawa Y, Sagane Y, Sakurai S-i, et al. Large-scale production of phospholipase D from Streptomyces racemochromogenes and its application to soybean lecithin modification[J]. Applied Biochemistry and Biotechnology,2011,165(7-8):1494−1506. doi: 10.1007/s12010-011-9370-4
[44]	Huang T T, Lv X Q, Li J H, et al. Combinatorial fine-tuning of phospholipase D expression by Bacillus subtilis WB600 for the production of phosphatidylserine[J]. Journal of Microbiology and Biotechnology,2018,28(12):2046−2056. doi: 10.4014/jmb.1806.06048
[45]	Fedeli C, Carrea G, Monti D. On the effects of site-specific mutations on activity and expression of the Streptomyces PMF phospholipase D[J]. Journal of Molecular Catalysis B: Enzymatic,2006,41(1-2):1−7. doi: 10.1016/j.molcatb.2006.03.004
[46]	陈可泉, 庞洋, 王昕一株产磷脂酶D的基因工程菌及其构建方法与应用: 中国, CN106957850A [P]. 2017-07-18.
[47]	徐银凤, 赵雨, 孙迪, 等. 蜡状芽孢杆菌磷脂酶D的活性形式及HKD活性区域的分子改造对其活性的影响[J]. 中国生物化学与分子生物学报,2017,33(11):1161−1167.
[48]	Ogino C, Daido H, Ohmura Y, et al. Remarkable enhancement in PLD activity from Streptoverticillium cinnamoneum by substituting serine residue into the GG/GS motif[J]. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics,2007,1774(6):671−678. doi: 10.1016/j.bbapap.2007.04.004
[49]	Ogino C, Kanemasu M, Fukumoto M, et al. Continuous production of phospholipase D using immobilized recombinant Streptomyces lividans[J]. Enzyme & Microbial Technology,2007,41(1-2):156−161.
[50]	韩海霞, 曹栋, 史苏佳, 等. 链霉菌CA-1产磷脂酶D发酵条件的优化[J]. 食品工业科技,2014,35(13):176−180.
[51]	刘逸寒, 薄嘉鑫, 乔婧, 等. 毕赤酵母表面展示磷脂酶D高密度发酵优化[J]. 食品研究与开发,2012,33(8):184−187. doi: 10.3969/j.issn.1005-6521.2012.08.055
[52]	Fukuda H, Turugida Y, Nakajima T, et al. Phospholipase D production using immobilized cells of Streptoverticillium cinnamoneum[J]. Biotechnology Letters,1996,18(8):951−956. doi: 10.1007/BF00154628

[1]	LIU Qiling, WANG Qingwei. Effects of Short- and Medium-wave Infrared Radiation Drying on Drying Characteristics, Nutritional Quality and Antioxidant Activity of Mulberry[J]. Science and Technology of Food Industry, 2021, 42(12): 39-45. DOI: 10.13386/j.issn1002-0306.2020090209
[2]	WANG Xiao-min, SHI Guan-ying, WANG Zhao-gai, ZHANG Le, CHENG Jing-jing, JIANG Peng-fei, ZHAO Li-li. Infrared Fingerprint Spectra Analysis of Toona sinensis Based on Sequential Dual-indexes and Cluster Analysis Method[J]. Science and Technology of Food Industry, 2019, 40(20): 231-236. DOI: 10.13386/j.issn1002-0306.2019.20.037
[3]	YANG Yang, GUO Qing-qi, ZHANG Na, LIU Li-jie, YANG Xiao-wan, WANG Bing, SHI Yan-guo. Relationship between the Structure and Solubility of Nano-Soybean Peptides Revealed by Infrared Spectroscopy and Atomic Force Microscopy[J]. Science and Technology of Food Industry, 2018, 39(22): 1-5. DOI: 10.13386/j.issn1002-0306.2018.22.001
[4]	WANG Qiong, CHU Li-jun, KOU Li-ping. Determination of polyphenols and flavonoids content in pomegranate peels by near infrared reflectance spectroscopy[J]. Science and Technology of Food Industry, 2017, (20): 292-296. DOI: 10.13386/j.issn1002-0306.2017.20.053
[5]	LU Liang, LI Jing-jing, ZHOU Zhao-lu, TIAN Shu-hua, HUANG Sheng-quan, HUANG Yan-sheng. The rapid determination of polysaccharides in oral liquid based on near infrared reflectance spectroscopy technique[J]. Science and Technology of Food Industry, 2017, (18): 247-251. DOI: 10.13386/j.issn1002-0306.2017.18.047
[6]	LIU Ling-ping, HE Xiao-ying, DU Li-hui, SHEN Fei, YUAN Jian, JU Xing-rong. Application of attenuated total reflection- fourier transform infrared spectroscopy for rapid identification of fungi strains on grain[J]. Science and Technology of Food Industry, 2016, (19): 298-301. DOI: 10.13386/j.issn1002-0306.2016.19.049
[7]	LI Yang, WANG Zhong-jiang, WANG Rui, SUI Xiao-nan, QI Bao-kun, HAN Fei-fei, BI Shuang, JIANG Lian-zhou. Fourier transform infrared spectroscopic analysis of soybean isolate protein at different heat treatment conditions[J]. Science and Technology of Food Industry, 2016, (08): 104-109. DOI: 10.13386/j.issn1002-0306.2016.08.013
[8]	ZHAO Wu-qi, SHI Ke-xin, GU Yue, JIANG Chang-song. Study on determination of acidity in pomegranate juice by near infrared spectroscopy[J]. Science and Technology of Food Industry, 2014, (16): 68-70. DOI: 10.13386/j.issn1002-0306.2014.16.006

Supplements (0)

Cited By

Cited by

Periodical cited type(2)

1.	涂玲飞，陈迎丽，李焱，张振. 白及多糖锌的结构表征及其抗氧化活性评价. 食品与发酵工业. 2024(17): 218-225+245 .
2.	宋林梦，孔烁，蔡雨情，高慧，余远，纪雪莹，陶飞燕，薛鹏. 基于响应面法优化弱酸热催化制备藜麦低极性皂苷及活性研究. 食品科技. 2023(09): 192-200 .