优质L-天冬酰胺酶的开发与应用及重组表达研究进展

doi:10.13523/j.cb.20171117

中国生物工程杂志

2017, Vol. 37

Issue (11): 123-131 DOI: 10.13523/j.cb.20171117

综述

优质L-天冬酰胺酶的开发与应用及重组表达研究进展

曾杰

江苏恒瑞医药股份有限公司国家靶向药物工程技术研究中心连云港 222047

Development and Application of L-Asparaginase with Better Performance and Advances in Recombinant Expression

ZENG Jie

Jiangsu Hengrui Medicine Co., Ltd., National Engineering Technology Research Center of Targeted Drugs, China, Lianyungang 222047, China

全文: PDF(493 KB) HTML

摘要： L-天冬酰胺酶用于治疗急性淋巴细胞白血病与淋巴瘤，但高昂的价格限制了临床上的广泛应用，重组表达解决了成本的难题。L-天冬酰胺酶所具有的低谷氨酰胺酶活性是其副作用的根源，同时细菌来源的L-天冬酰胺酶能导致危及生命的过敏反应，寻找副作用更低的优质L-天冬酰胺酶及其修饰方法，成为研究的重点。对L-天冬酰胺酶的重组表达，及具有更优性质的L-天冬酰胺酶开发进展进行了综述，并阐明其在临床治疗及食品工业领域的巨大应用潜力。

关键词： 急性淋巴细胞白血病; 丙烯酰胺; 天冬酰胺酶; 重组表达; 毒副作用

Abstract: L-asparaginase is an anti-neoplastic agent, used in acute lymphoblastic leukemia(ALL) and lymphosarcoma chemotherapy. However, the application in clinic therapeutics is obstructed by its high costs of production. Nevertheless, the expression system of recombinant proteins have solved this problem perfectly. The intrinsic low-rate glutaminase activity of L-asparaginase, however, causes serious side-effects. In addition, L-asparaginase from bacterial origin can cause hypersensitivity in the long-term used, leading to allergic reactions and anaphylaxis. The search for new L-asparaginase sources, which shows less adverse effects, has become the focus of scholar studies. A review of recent progress in development of L-asparaginase with better performance are presented. Furthermore, the successful expression of recombinant L-asparaginase were aslo summarized and analyzed, and the potential perspective of L-asparaginase to be used in clinic therapeutics and food industry was discussed.

Key words: Reducing adverse effects Acrylamide L-asparaginase Recombinant expression Acute lymphoblastic leukemia

收稿日期: 2017-05-02 出版日期: 2017-11-15

ZTFLH:

Q81

通讯作者: 曾杰 E-mail: zeng2408@163.com

	服务
	把本文推荐给朋友
	加入引用管理器
	E-mail Alert
	RSS
	作者相关文章
	曾杰

引用本文:

曾杰. 优质L-天冬酰胺酶的开发与应用及重组表达研究进展[J]. 中国生物工程杂志, 2017, 37(11): 123-131.

ZENG Jie. Development and Application of L-Asparaginase with Better Performance and Advances in Recombinant Expression. China Biotechnology, 2017, 37(11): 123-131.

链接本文:

https://manu60.magtech.com.cn/biotech/CN/10.13523/j.cb.20171117 或 https://manu60.magtech.com.cn/biotech/CN/Y2017/V37/I11/123

[1]	Kidd J G. Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum. I. Course of transplanted cancers of various kinds in mice and rats given guinea pig serum,horse serum or rabbit serum. Journal of Experimental Medicine,1953,98(6):565-582.
[2]	Broome J D. Evidence that the L-asparaginase activity of guinea pig serum is responsible for its anti-lymphoma effects. Nature,1961,191:1114-1115.
[3]	Mashburn L T,Wriston J C. Tumor inhibitory effect of L-asparaginase from Escherichia coli. Archives of Biochemistry and Biophysics,1964,105:450-452.
[4]	Campbell H A,Mashburn L T,Boyse E A,et al.Two Asparaginase from Escherichia coli B,their separation,purification and antitumor property. Biochemistry,1967,6(3):721-730.
[5]	Swain A L,Jaskolski M,Housset D,et al. Crystal structure of Escherichia coli L-asparaginase,an enzyme used in cancer therapy. Proceedings of the National Academy of Sciences of the United States of America,1993,90(4):1474-1478.
[6]	Ahmad N,Pandit N P,Maheshwari S K. L-asparaginase gene-a therapeutic approach towards drugs for cancer cell. International Journal of Biosciences,2012,2(4):1-11.
[7]	Jha S K,Pasrija D,Sinha R K,et al. Microbial L-asparaginase:a review on current scenario and future prospects. International Journal Pharmaceutical Sciences and Research,2012,3(9):3076-3090.
[8]	Pieters R,Hunger S P,Boos J,et al. L-asparaginase treatment in acute lymphoblastic leukemia. Cancer,2011,117(2):238-249.
[9]	Prihanto A A,Wakayama M. Marine microorganism:an underexplored source of L-asparaginase. Advances in Food and Nutrition Research,2016,79:1-25.
[10]	Cedar H,Schwartz J H. Production of L-asparaginase Ⅱ by Escherichia coli. Journal of Bacteriology,1968,96(6):2043-2048.
[11]	Jennings M P,Beacham I R.Analysis of the Escherichia coli gene encoding L-asparaginase Ⅱ,ansB,and its regulation by cyclic AMP receptor and FNR proteins. Journal of Bacteriology,1990,172(3):1491-1498.
[12]	Younes G,Alireza E,Sara R A,et al. An optimized medium for screening of L-asparaginase production by Escherichia coli. American Journal of Biochemistry and Biotechnology,2008,4(4):422-424.
[13]	Varalakshmi V,Raju K J. Optimization of L-asparaginase production by Aspergillus terreus MTCC 1782 using bajra seed flour under solid state fermentation. International Journal of Research in Engineering and Technology,2013,2(9):121-129.
[14]	Vijay B,Raju K J. Production of L-asparaginase by Aspergillus terreus MTCC 1782 under solid state fermentation using pearl millet and finger millet as mixed substrate. Journal of Chemical,Biological and Physical Sciences,2015,5(1):366-377.
[15]	Khushoo A,Pal Y,Mukherjee K J. Optimization of extracellular production of recombinant asparaginase in Escherichia coli in shake-flask and bioreactor. Appl Microbiol Biotechnol,2005,68(2):189-197.
[16]	Shokri A,Sanden A M,Larsson G. Growth rate-dependent changes in Escherichia coli membrane structure and protein leakage. Appl Microbiol Biotechnol,2002,58(3):386-392.
[17]	Aghaeepoor M,Mozafari S,Shahrakl M K,et al. High level of extracellular fermentation and alternative purification of Escherichia coli Asparaginase Ⅱ. Biharean Biologist,2011,5(2):96-101.
[18]	Upadhyay A K,Singh A,Mukherjee K J,et al. Refolding and purification of recombinant L-asparaginase from inclusion bodies of E.coli into activetetrameric protein. Frontiers in Microbiology,2014,5:486.
[19]	Ghoshoon M B,Berenjian A,Hemmati S,et al. Extracellular production of recombinant L-asparaginase Ⅱ in Escherichia coli:medium optimization using response surface methodology. International Journal of Peptide Research and Therapeutics,2015,21(4):487-495.
[20]	Zhang K,Su L Q,Duan X G,et al. High-level extracellular protein production in Bacillus subtilis using an optimized dual-promoter expression system. Microbial Cell Factories,2017,16(1):32.
[21]	Feng Y,Liu S,Jiao Y,et al. Enhanced extracellular production of L-asparaginase from Bacillus subtilis 168 by B. Subtilis WB600 through a combined strategy. Applied Microbiology and Biotechnology,2017,101(4):1509-1520.
[22]	Doriya K,Kumar D S. Isolation and screening of L-asparaginase free of glutaminase and urease from fungal sp. Biotech,2016,6(2):239.
[23]	Ferrara M A,Severino N M,Mansure J J,et al. Asparaginase production by a recombinant Pichia pastoris strain harbouring Saccharomyces cerevisiae ASP3 gene. Enzyme and Microbial Technology,2006,39(7):1457-1463.
[24]	Facchinetti C G,Gonçalves R S,Sobral R S,et al. Saccharomyces cerevisiae asparaginase Ⅱ,a potential antileukemic drug:Purification and characterization of the enzyme expressed in Pichia pastoris. Protein Expression and Purification,2016,120:118-125.
[25]	Costa I M,Schultz L,Araujo B P,et al. Recombinant L-asparaginase 1 from Saccharomyces cerevisiae:an allosteric enzyme with antineoplastic activity. Scientific Reports,2016,6:36239.
[26]	Pourhossein M,Korbekandi H. Cloning,expression,purification and characterisation of Erwinia carotovora L-asparaginase in Escherichia coli. Advanced Biomedical Research,2014,3:82.
[27]	Chityala S,Venkata D V,Ahmad J,et al. High yield expression of novel glutaminase free L-asparaginase Ⅱ of Pectobacterium carotovorum MTCC 1428 in Bacillus subtilis WB800N. Bioprocess and Biosystems Engineering,2015,38(11):2271-2284.
[28]	Meena B,Anburajan L,Vinithkumar N V,et al. Molecular expression of l-asparaginase gene from Nocardiopsis alba NIOT-VKMA08 in Escherichia coli:A prospective recombinant enzyme for leukaemia chemotherapy. Gene,2016,590(2):220-226.
[29]	Lee S J,Lee Y,Park G H,et al. A newly identified glutaminase-free L-asparaginase (L-ASPG86) from the marine bacterium Mesoflavibacter zeaxanthinifaciens. Journal of Microbiology and Biotechnology,2016,26(6):1115-1123.
[30]	Nagarajan A,Thirunavukkarasu N,Suryanarayanan T S,et al. Screening and isolation of novel glutaminase free L-asparaginase from fungal endophytes. Research Journal of Microbiology,2014,9(4):163-176.
[31]	Xu F,Oruna C M,Elmore J S. The use of asparaginase to reduce acrylamide levels in cooked food. Food Chemistry,2016,210:163-171.
[32]	Zyzak D V,Sanders R A,Stojanovic M,et al. Acrylamide formation mechanism in heated foods. Journal of Agricultural and Food Chemistry,2003,51(16), 4782-4787.
[33]	Jia M,Xu M,He B,et al. Cloning,expression,and characterization of L-asparaginase from a newly isolated Bacillus subtilis B11-06. Journal of Agricultural and Food Chemistry,2013,61(39):9428-9434.
[34]	Hong S J,Lee Y H,Khan A R,et al. Cloning,expression,and characterization of thermophilic L-asparaginase from Thermococcus kodakarensis KOD1. Journal of Basic Microbiology,2014,54(6):500-508.
[35]	Huang L,Liu Y,Sun Y,et al. Biochemical characterization of a novel L-asparaginase with low glutaminase activity from Rhizomucor miehei and its application in food safety and leukemia treatment. Applied and Environmental Microbiology,2014,80(5):1561-1569.
[36]	Song P,Wang Z,Zhang X,et al. The role of autophagy in asparaginase-induced immune suppression of macrophages. Cell Death & Disease,2017,8(3):e2721.
[37]	Sakaguchi S,Higa T,Suzuki M,et al. Prophylactic use of octreotide for asparaginase-induced acute pancreatitis. International Journal of Hematology, 2017:1-3.
[38]	Bahreini E,Aghaiypour K,Abbasalipourkabir R,et al. Preparation and nanoencapsulation of L-asparaginase Ⅱ in chitosan-tripolyphosphate nanoparticles and in vitro release study. Nanoscale Research Letters,2014,9(1):340.
[39]	Baskar G,Chandhuru J,Sheraz F K,et al. Anticancer activity of fungal L-asparaginase conjugated with zinc oxide nanoparticles. Journal of Materials Science-Materials in Medicine,2015,26(1):5380.
[40]	Kim K,Jeong J H,Lim D,et al. L-Asparaginase delivered by Salmonella typhimurium suppresses solid tumors. Molecular Therapy Oncolytics,2015,2(C):15007.
[41]	Wang Y,Qian S,Meng G,et al. Cloning and expression of L-asparaginase gene in Escherichia coli.Applied Biochemistry and Biotechnology,2001,95(2):93-101.
[42]	Roth G,Nunes J E,Rosado L A,et al. Recombinant Erwinia carotovora L-asparaginase Ⅱ production in Escherichia coli fed-batch cultures. Brazilian Journal of Chemical Engineering,2013,30(2):245-256.

[1]	袁小晶,尹海梦,樊晓玮,何俊林,郝石磊,季金苟. 角蛋白/海藻酸钠/聚丙烯酰胺水凝胶皮肤敷料的制备及创口修复研究[J]. 中国生物工程杂志, 2021, 41(8): 17-24.
[2]	王惠临,周凯强,朱红雨,王力景,杨仲璠,徐明波,曹荣月. 凝血因子VII及其重组表达新进展[J]. 中国生物工程杂志, 2021, 41(2/3): 129-137.
[3]	陈素芳,夏明印,曾丽艳,安晓琴,田敏芳,彭建. 抗菌肽Cec4a的重组表达和抗菌活性研究^*[J]. 中国生物工程杂志, 2021, 41(10): 12-18.
[4]	乐易林,傅毓,倪黎,孙建中. 热稳定性丙酮酸:铁氧还蛋白氧化还原酶异源表达及其在乙酰辅酶A合成中的应用 ^*[J]. 中国生物工程杂志, 2020, 40(3): 72-78.
[5]	薛瑞,姚林,王瑞,罗正山,徐虹,李莎. 重组贻贝足蛋白的研究进展与应用^*[J]. 中国生物工程杂志, 2020, 40(11): 82-89.
[6]	陈曼,王爱先,傅旻婧,吴雪英,甄军毅,宫美维,郭亚,王卉. CAR细胞疗法在T细胞-急性淋巴细胞白血病应用的新进展[J]. 中国生物工程杂志, 2019, 39(9): 103-107.
[7]	韩挺翰,龚雪梅,郦娟,丁亚芳,卢辰,张坤晓,高嵩,许恒皓. 一种来源于大菱鲆的热敏型尿嘧啶DNA糖苷酶的克隆表达及酶学性质鉴定 ^*[J]. 中国生物工程杂志, 2019, 39(10): 34-43.
[8]	王曦,张光德,陈熙明,浦铜良. 溶葡球菌酶在乳酸克鲁维酵母中重组表达、诱变、优化及酶学研究^*[J]. 中国生物工程杂志, 2017, 37(12): 49-58.
[9]	饶菁菁, 景一娴, 邹明月, 胡小蕾, 廖飞, 杨晓兰. 季也蒙毕赤酵母菌尿酸酶基因的克隆、重组表达及表征[J]. 中国生物工程杂志, 2017, 37(11): 74-82.
[10]	赵一瑾, 王腾飞, 汪俊卿, 王瑞明. 以CotC为分子载体在枯草芽孢杆菌表面展示海藻糖合酶[J]. 中国生物工程杂志, 2017, 37(1): 71-80.
[11]	李梦悦, 王腾飞, 汪俊卿, 赵一瑾, 程成, 王瑞明. 海藻糖合酶在毕赤酵母表面的展示[J]. 中国生物工程杂志, 2016, 36(2): 73-80.
[12]	丁一, 吴海英, 史吉平, 孙俊松. 氢化酶重组表达研究进展[J]. 中国生物工程杂志, 2015, 35(5): 109-118.
[13]	杨波, 陈海琴, 宋元达, 张灏, 陈卫. 动物双歧杆菌肌球交叉反应抗原MCRA酶学功能的研究[J]. 中国生物工程杂志, 2012, 32(12): 30-36.
[14]	高炳淼, 李宝珠, 吴勇, 林波, 朱晓鹏, 长孙东亭, 罗素兰. 重组芋螺毒素GeXIVAWT的表达、纯化和鉴定[J]. 中国生物工程杂志, 2012, 32(09): 34-40.
[15]	周罡, 杨君, 杨青. 亚洲玉米螟的O-β-N-氨基乙酰葡萄糖基水解酶 (OfOGA)的基因克隆及重组表达[J]. 中国生物工程杂志, 2012, 32(05): 36-42.

Viewed

Full text

Abstract

Cited

Shared

Discussed