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Type :thesis
Subject :QR Microbiology
Main Author :Suzana Adenan
Title :Isolation and characterization of new thermophilic aminoacylase from Geobacillus sp. Strain Szn
Place of Production :Tanjong Malim
Publisher :Fakulti Sains dan Matematik
Year of Publication :2018
Corporate Name :Universiti Pendidikan Sultan Idris
PDF Guest :Click to view PDF file
PDF Full Text :Click to view PDF file

Abstract : Universiti Pendidikan Sultan Idris
Kajian  ini  bertujuan  untuk  memencilkan  dan  mencirikan  aminoasilase  termostabil daripada bakterium termofilik.  Dalam pemencilan bakterium, sampel air dan sedimen telah   diperolehi   dari  Air  Panas  Ulu  Slim,  Perak.  Aminoasilase   SZN  termostabil diekstrak   secara intrasellular dan ditulenkan sehingga homogen dengan menggunakan kromatografi   pertukaran    ion  dan  pengasingan   saiz  dalam  eksperimen   seterusnya. Aminoasilase  SZN yang tulen telah  dicirikan pada pelbagai  suhu, pH, ion logam dan perencat.  Kajian  struktur  lebih  lanjut   menggunakan  spektrokopi  sirkular  dikroisma dilakukan  bagi menentukan  kestabilan  a-heliks dan  lembaran     dalam pelbagai  suhu. Penghasil    aminoasilase    termofilik    yang    dipencilkan     itu    dikenalpasti    sebagai Geobacillus  sp.  strain  SZN.  Aminoasilase  SZN  dicirikan   sebagai  enzim  termostabil dengan  aktiviti  optimum  pada  60°C,  pH  7.5,  tempoh  separuh   hayat  16  jam  dengan peningkatan  aktiviti  dan  kestabilan  dalam  beberapa  ion  logam  dan   perencat  yang diuji.  Keputusan  daripada  penentuan  struktur  menunjukkan   pengurangan    a-heliks secara   beransur-ansur   daripada   36   hingga   27.6%,   diikuti   dengan    disorientasi mendadak   struktur  tersebut  pada  peralihan   suhu  daripada  60  hingga  70°C   (27.6 hingga 19.5%). Sebaliknya, peratusan  lembaran   ,  telah meningkat  secara stabil pada suhu  yang diuji. Struktur a-heliks yang juga merupakan  lokasi residu-residu  pengikat logam dan  pemangkin  yang penting, lemah sepenuhnya pada suhu melebihi 70°C lalu mengakibatkan  kehilangan  aktiviti. Kesimpulannya, aminoasilase  SZN telah dicirikan sebagai   enzim   termostabil    berdasarkan   kepada   integriti   struktur   a-heliks   dan kestabilan  fungsinya  pada  suhu   tinggi.  Implikasi  kajian  ini  menunjukkan   bahawa aminoasilase  SZN  mampu  menjadi  enzim   altematif  kepada  bioindustri  berdasarkan kepada  peningkatan  aktiviti  enzim  dalam  suhu   tinggi  dan  kestabilan  dalam  pelbagai perencat yang diuji.  


Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., &

Lipman, D. J. (1997). Gapped BLAST and PSI-BLAST: a new generation

of protein database search programs. Nucleic Acids Research, 25, 3389-



Amend, J.P., Rogers, K.L., Shock, E.L., Gurrieri, S., & Inguaggiato, S. (2003)

Energetics of chemolithoautotrophy in the hydrothermal system of Vulcano

Island, southern Italy. Geobiology, 1,37-58.


Ash, C., Farrow, J.A.E., Wallbanks, S., & Collins, M.D. (1991). Phylogenetic

heterogeneity of the genus Bacillus revealed by comparative analysis of

small-subunit-ribosomal RNA sequences. Letters in Applied

Microbiology,13, 202-206.


Bakker, M., Spruijt, A.S., Rantwijk, V. F. & Sheldon, R.A. (2000). Highly

enantioselective aminoacylase-catalyzed transesterification of secondary

alcohols. Tetrahedron: Asymmetry, 11, 1801-1808.


Barrett, A. J. (1994). Classification of peptidases. Methods in Enzymology, 244,1-15.


Bhattacharya, S., Chattopadhyay, D., Raha, S., Mukhopadhyay, A., & Division, M. B.

(2012). International journal of institutional pharmacy and life sciences, 2,



Bradford, M. M., (1976). A rapid and sensitive method for the quantification of

microgram quantities of protein utilizing the principles of protein-dye binding.

Analytical Biochemistry, 72, 248-254.


Brown, R., Toogood, H. S., Hollingsworth, E. J., Brown, R. C., Taylor, I. N., Taylor,

S. J. C. et al (2002). A thermostable L-aminoacylase from Thermococcus

litoralis : Cloning, overexpression, characterization, and applications in

biotransformations. Extremophiles, 6(2), 111-22.


Bryant, M. (2003). Biosynthesis of amino acids. Retrieved from


Cho, H. Y., Tanizawa, K., Tanaka, H., & Soda, K. (1987). Thermostable

aminoacylase from Bacillus thermoglucosidius: purification and

characterization. Agricultural Biology Chemistry, 51, 2793- 2800.


Cihan, A.C., Tekin, N., Ozcan, B., & Cokmus, C. (2012). The Genetic Diversity Of

Genus Bacillus And The Related Genera Revealed by 16S rRNA Gene

Sequences and Ardra Analyses Isolated from Geothermal Regions of

Turkey. Brazilian Journal of Microbiology, 43(1), 309–324.


Curley, P., Does, C., Dreissen, A. M., Kok, J., & Sinderen, D. V. (2003). Purification

and characterisation of a lactococcal aminoacylase. Archieve

Microbiology, 179, 402-408.


Deleage G., & Geourjon. C. (1995). SOPMA: significant improvements in protein

secondary structure prediction by concensus prediction from multiple

allignments. Computer Applications in the Biosciences, 11(6), 681-684.


Derekova, A., Mandeva, R., & Kambourova, M. (2008). Phylogenetic diversity of

thermophilic carbohydrate degrading bacilli from Bulgarian hot springs.

World Journal of Microbiology and Biotechnology, 24, 1697-1702.


Faraldos, J., Arroyo, E., & Herradón, B. (1997). Biocatalysis in organic synthesis.

Highly enantioselective kinetic resolution of secondary alcohols catalyzed

by acylase. Synlett, 9, 367-370.


Gasteiger, E., Gattiker, A., Hoogland, C., Ivanyi, I., Appel, R. D., & Bairoch, A.

(2003). ExPASy: the proteomics server for in-depth protein knowledge and

analysis. Nucleic Acids Research, 31, 3784-3788.


Greenfield, N. J. (2009). Using circular dichroism spectra to estimate protein

secondary structure. Nature Protocols, 1(6), 2876–2890.


Handbook of Proteolytic Enzymes. (1998). London: Academic Press.


Hickey, D.A., & Singer, G.A. (2004). Genomic and proteomic adaptations to growth

at high temperature. Genome Biology 5, (117), 1-117.


Holt, K. (2004). Biocatalysis and chemocatalysis - a powerful combination for the

preparation of enantiomerically pure α-amino acids. Pharmachem 3, 2–4.


Hsu, C., Lai, W., Chang, W., & Liaw, S. (2002). Structural-based mutational analysis

of D -aminoacylase from Alcaligenes faecalis DA1, Protein Science, 11,



Huffer, S., Clark, M.E., Ning, J.C., Blanch, H.W., & Clark, D.S. (2011). The Role of

Alcohols in Growth, Lipid Composition, and Membrane Fluidity of Yeast,

Bacteria, and Archaea. Applied and Environmental Microbiology. 77(18),



Hurst, L.D., & Merchant, A.R. (2001). High guanine-cytosine content is not an

adaptation to high temperature: a comparative analysis amongst

prokaryotes. Proceedings. Biological sciences Royal Society, 268, (1466),



Ishikawa, K., Ishida, H., Matsui, I., Kawarabayasi, Y., & Kikuchi, H. (2001). Novel

bifunction hyperthermostable carboxypeptidase/aminoacylase from

Pyrococcus horikoshii OT3. Applied and Environmental Microbiology, 67,



Ivanov, K., Stoimenova, A., Obreshkova, D., & Saso, L. (2014). Biotechnology in the

Production of Pharmaceutical Industry Ingredients: Amino Acids.

Biotechnology & Biotechnological Equipment, 27(2), 3620-3626.


Joo, H.-S., and Choi, J. W. (2012). Purification and characterization of a novel

alkaline protease from Bacillus horikoshii. Journal

of Microbiology and Biotechnology, 22(1), 58–68.


Jozic, D., Bourenkow, G., Bartunik, H., Scholze, H., Dive, V., Henrich, et al (2002).

Crystal structure of the dinuclear zinc aminopeptidase PepV from

Lactobacillus delbrueckii unravels its preference for dipeptides. Structure, 10

(8), 1097–1106.


Kokkinidis, B. M., Glykos, N. M., & Fadouloglou, V. E. (2012). Chapter 7 - Protein

Flexibility and Enzymatic Catalysis. Advances in Protein Chemistry and

Structural Biology, 87: 181-218.


Koreishi, M., Asayama, F., Imanaka, H., Imamura, K., Kadota, M., Tsuno, T., &

Nakanishi, K. (2005). Purification and characterization of a novel

aminoacylase from Streptomyces mobaraensis. Bioscience, Biotechnology,

and Biochemistry, 69(10), 1914–1922.


Koreishi, M., Nakatani, Y., Ooi, M., Imanaka, H., Imamura, K., & Nakanishi, K.

(2009). Purification , Characterization , Molecular Cloning , and Expression of

a New Aminoacylase from Streptomyces mobaraensis That Can Hydrolyze

N - (Middle / Long) -chain-fatty-acyl-L-amino Acids as Well as N -Shortchain-

acyl-L-amino acids. Bioscience, Biotechnology, and Biochemistry, 73

(9), 1940–1947.


Kramers, H.A. (1940). Brownian motion in a field of force and the diffusion model of

chemical reactions. Physica, 7,284–304.


Kumar, S., & Nussinov, R. (1999). Salt bridge stability in monomeric proteins.

Journal of Molecular Biology, 293, 1241–1255.


Kumar, S., Stecher, G., & Tamura, K. (2016). MEGA7 : Molecular Evolutionary

Genetics Analysis version 7.0 for bigger datasets MEGA7. Molecular

Biology and Evolution, 33(7),1870–1874.


Kyte, J., & Doolittle, R. F. (1982). A simple method for displaying the hydropathic

character of protein. Journal of Molecular Biology,157, 105-132.


Liljeblad, A., Aksela, R., and Kanerva, L.T. (2001). Use of enantio-, chemo- and

regioselectivity of acylase I. Resolution of polycarboxylic acid esters.

Tetrahedron Asymmetry, 12, 2059-2066.


Lin, L. L., Chen, M. H., Chien, H. C., Kan, S. C., Chen, C. C., Hu, H. Y., & Hsu, W.

H. (2007). Characterization of abifunctional aminoacylase/carboxypeptidase

from radioresistant bacterium Deninococcus radiodurans R1. Journal of

Biotechnology, 128, 322-334.


Lindner, H. A., Lunin, V. V, Alary, A., Hecker, R., & Cygler, M. (2003). Essential

Roles of Zinc Ligation and Enzyme Dimerization for Catalysis in the

Aminoacylase-1 /M20 Family. Journal of Biological Chemistry, 278(45),



Littlechild, J. A. (2015). Enzymes from extreme environments and their industrial

applications. Process and Industrial Biotechnology, 3(161), 1–9.


Logan, N.A., Berge, O., Bishop, A,H., Busse, H.J., de Vos, P. et al (2009). Proposed

minimal standards for describing new taxa of aerobic, endospore- forming

bacteria. International Journal of Systematic and Evolutionary Microbiology,

59, 2114–2121.


Ludwig, W., Schleifer, K.H., & Whitman, W.B. (2007). Revised road map to the

phylum Firmicutes. Bergey’s Manual Trust website


Madigan, M.T. & Martino, J.M. (2006). Brock Biology of Microorganisms (11th ed.).

p:136. Pearson.


Mallick, P., Boutz, D.R., Eisenberg, D., & Yeates, T.O. (2002). Genomic evidence

that the intracellular proteins of archaeal microbes contain disulfide

bonds. Proceedings of the National Academy of Sciences,99, 9679–



Marguet, E., & Forterre, P. (1998). Protection of DNA by salts against

thermodegradation at temperatures typical for hyperthermophiles.

Extremophiles, 2, 115-122.


Martínez-rodríguez, S., García-pino, A., Las, J., Clemente-jiménez, J. M., Rodríguezvico,

F., García-ruiz, J. et al (2012). Mutational and Structural Analysis of L -

N -Carbamoylase Reveals New Insights into a Peptidase M20 / M25 / M40

Family Member. Journal of Bacteriology,194 (21), 5759–5768.


McKee, T., & McKee, J. R., (2003). Enzymes. In: Biochemistry: The molecular

basis of life, (3rd edition), New York, USA. pp: 161-199: McGraw-

Hill Higher Education.


Miller. (1972). Experiments in molecular genetics. Cold Spring Harbor Laboratory,

Cold Spring Harbor, N.Y.


Miñana-Galbis, D., Pinzón, D.L., Lorén, J.G., Manresa, A., & Oliart-Ros, R.M.

(2010). Reclassification of Geobacillus pallidus as Aeribacillus pallidus gen.

nov., comb. Nov. International Journal of Systematic and Evolutionary

Microbiology, 60, 1600-1604.


Minasov, G., Shuvalova, L., Brunzelle, J.S., Collart, F.R., Anderson, W.F., &

Midwest (unpublished). Crystal Structure of Bacillus Subtilis YXEP

Protein (APC1829), a Dinuclear Metal Binding Peptidase from M20

Family Center for Structural Genomics (MCSG).


Moore, S. & Stein, W.H. (1948). Photometric Ninhydrin Method for Use in The

Chromatography of Amino Acids. Journal of Biological Chemistry, 176, 367-



Muñiz-Lozano, F., Domιnguez-Sánchez, G. & Dιaz-Viveros, Y. (1998). DAminoacylase

from a novel producer: Stenotrophomonas maltophilia ITV-

059521: 296. The Journal of Industrial Microbiology and Biotechnology, 21

(6), 296–299.


Nakagawa, S., & Takai, K. (2006). The isolation of thermophiles from deep-sea

hydrothermal environments. In Methods in Microbiology: Extremophiles

(Eds). New York, NY, USA: Elsevier.


Natali, V., Russo, D., Estrin, D.A., Marti, M.A., & Roitberg, A.E. (2012). pHDependent

Conformational Changes in Proteins and Their Effect on

Experimental pK a s : The Case of Nitrophorin. PLOS Computational Biology,



Nazina, T.N., Tourova, T.P., Poltaraus, A.B., Novikova, E.V., Grigoryan, A.A.,

Ivanova, A.E., Lysenko, A.M., Petrunyaka, V.V., Osipov, G.A., Belyaev, S.S.,

Ivanov, M.V. (2001). Taxonomic study of aerobic thermophilic bacilli:

descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus

uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus

stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans,

Bacillus kaustophilus, Bacillus thermoglucosidius and Bacillus

thermodenitrificans to Geobacillus as the new combinations G.

stearothermophilus, G. thermocatenulatus, G. thermoleovorans,G.

kaustophilus, G. thermoglucosidasius and G.thermodenitrificans. International

Journal of Systematic Evolutionary Microbiology, 51, 433-446.


Otieno, D. O. (2010). Synthesis of β -Galactooligosaccharides from Lactose Using

Microbial β –Galactosidases. Food Science & Technology, 9, 471–482.


Pace, N.R. 1997. L- and D- Amino Acids The biology place. Science, 276, 734–740.

Retrieved from

bioprop/landd.html : Pearson Education


Parker B. M., Taylor I. N., Woodley J. M., Ward J. M. & Dalby P.A. (2011). Directed

evolution of a thermostable l-aminoacylase biocatalyst. Journal of

Biotechnology, 155 (4), 396-405.


Patel, R. N. (2013). Biocatalytic Synthesis of Chiral Alcohols and Amino Acids for

Development of Pharmaceuticals. Biomolecules,3, 741–777.


Petersen, T.N., Brunak, S., von Heijne, G.,& Nielsen, H. (2011). SignalP 4.0:

discriminating signal peptides from transmembrane regions. Nature Methods,



Rainey, F.A., Fritze, D., & Stackebrandt, E. (1994). The phylogenetic diversity of

thermophilic members of the genus Bacillus as revealed by 16S rRNA

analysis. FEMS Microbiology Letters,115, 205-211.


Raja Noor Zaleha Rahman Raja Abdul Rahman, Geok, Mahiran Basri, & Abu Bakar

Salleh, (2006). An organic solvent-stable alkaline protease from Pseudomonas

aeruginosa strain K: Enzyme purification and characterization. Enzyme and

Microbial Technology. 39,1484-1491


Rampelotto, P. H. (2010). Resistance of Microorganisms to Extreme Environmental

Conditions and Its Contribution to Astrobiology. Sustainability, 2, 1602-1623.


Raussens, V., Ruysschaert, J.M., & Goormaghtigh, E. (2003). Protein concentration is

not an absolute prerequisite for the determination of secondary structure from

circular dichroism spectra: a new scaling method. Analytical Biochemistry,



Raval, V. H., Rawal, C. M., Pandey, S., Bhatt, H. B., Dahima, B. R., & Singh, S. P.

(2014). Cloning, heterologous expression and structural characterization of an

alkaline serine protease from sea water haloalkaliphilic bacterium. Annals of

Microbiology. 65(1), 371–381.


Rawlings, N.D., Morton, F.R., Kok, C.Y., Kong, J., & Barrett, A.J. (2008). MEROPS:

the peptidase database. Nucleic Acids Research,36, 320–325.


Razvi, A., & Scholtz, J. M. (2006). Lessons in stability from thermophilic proteins.

Protein Science, 15,1569–1578. (2018). Amino Acids Market : Global Demand Analysis &

Opportunity Outlook 2024. Retrieved from amino-acids-market-global-demandanalysis-



Research & Market. (2015). Amino Acids Market Analysis By Product (LGlutamate,

Lysine, Methionine, Threonine, Tryptophan, Leucine, Iso-

Leucine, Valine, Glutamine, Arginine, Glycine, Phenylalanine, Tyrosine,

Citrulline, Creatine, Proline, Serine), By Source (Plant-Based & Animal-

Based), By Application (Animal Feed, Food & Dietary Supplements &

Pharmaceuticals) And Segment Forecasts To 2022. Amino Acids Market

Size, Share, Trends, Global Industry Report, 2022. Retrieved from


Robinson, P. K. (2015). Enzymes : principles and biotechnological applications,

Essays Biochem. (2015) 59, 1–41.


Rosen, H. (1957). A modified ninhydrin colorimetric analysis for amino acids.

Archieve Biochemistry & Biophysics, 67,10-15.


Saitou, N., & Nei, M. (1987). The neighbor-joining method—a new method for

reconstructing phylogenetic trees. Molecular Biology and Evolution, 4,406–



Sakanyan, V., Desmarez, L., Legrain, C., Charlier, D., Mett, I., & Kochikyan, A. et al

(1993). Gene cloning, sequence analysis, purification, and characterization of

a thermostable aminoacylase from Bacillus strearothermophilus. Applied and

Environmental Microbiology, 59, 3878-3888.


Schiraldi, C., Giuliano, M., & Rosa, M. D. E. (2002). Perspectives on

biotechnological applications of archaea. Archaea, 1, 75–86.


Shock, E.L., McCollom, T., & Schulte, M.D. (1998). Thermophiles: the Keys to

Molecular Evolution and the Origin of Life. 59–76.


Stetter, K. O. (1996). Hyperthermophile Prokaryotes. FEMS Microbiology Reviews,



Story, S. V., Grunden, A. M., & Adams, M. W. (2001). Characterization of an

aminoacylase from the hyperthermophilic archaeon Pyrococcus

furiosus. Journal of Bacteriology, 183, 4259-4268.


Subramaniam, S. (1998). The Biology Workbench: a seamless database and analysis

environment for the biologist. Proteins, 32, 1-2.


Tamura, K., Nei, M., & Kumar, S. (2004). Prospects for inferring very large

phylogenies by using the neighborjoining method. Proceedings of the

National Academy of Sciences (USA) 101,11030-11035.


Tanimoto, K., Higashi, N., Nishioka, M., Ishikawa, K., & Taya, M. (2008).

Characterization of thermostable aminoacylase from hyperthermophilic

archaeon Pyrococcus horikoshii, Federation of European Biochemical

Societies Journal , 275, 1140–1149.


Taylor, I.N., Brown, R.C., Bycroft, M., King, G., Littlechild, J.A., Lloyd, M.C. et al

(2004). Application of thermophilic enzymes in commercial biotransformation

processes. Biochemical Society Transactions, 32(2).


Ulrih, N.P., Gmajner, D., & Raspor, P. (2009). Structural and physico- chemical

properties of polar lipids from thermophilic archaea. Applications of

Microbiologyand Biotechnolology, 84,249–260.


Unsworth, L. D., Oost, J. Van Der, & Koutsopoulos, S. (2007). Hyperthermophilic

enzymes stability, activity and implementation strategies for high

temperature applications. Federation of European Biochemical Societies, 274,



Uribe, S., & Sampedro, J. G. (2003). Measuring Solution Viscosity and its Effect on

Enzyme Activity. Biological Procedures Online, 5(1),108–115. Vieille, C., &


Zeikus, G. J., (2001). Hyperthermophilic Enzymes: Sources Uses and Molecular

Mechanisms for Thermostability Hyperthermophilic Enzymes: Sources, Uses,

and Molecular Mechanisms for Thermostability. Microbiology and Molecular

Biology Reviews, 65(1),1–43.


Vieille, C., Burdette, D. S., & Zeikus, J. G. (1996). Thermozymes. Biotechnology

Annual Report, 2,1–83.


Vieille, C., Zeikus, G. J., & Vieille, C. (2001). Hyperthermophilic Enzymes : Sources

Uses and Molecular Mechanisms for Thermostability. Microbiology and

Molecular Biology Reviews, 65(1): 1–43.


Wardenga, R., Lindner, H. A., Hollmann, F., Thum, O., & Bornscheuer, U. (2010).

Biochimie Increasing the synthesis / hydrolysis ratio of aminoacylase 1 by

site-directed mutagenesis. Biochimie, 92(1), 102–109.


Weiß, H. M., Palm, G. J., & Rohm, K. (1995). Thermostable Aminoacylase from

Bacillus stearothermophilus : Significance of the Metal Center for Catalysis

and Protein Stability. Biological chemistry Hoppe-Seyler, 376, 643–649.


Wong, C. F, Noor, R., Raja, Z., Rahman, A., Salleh, A. B., & Basri, M. (2017).

Construction of New Genetic Tools as Alternatives for Protein Overexpression

in Escherichia coli and Pseudomonas aeruginosa. Iranian Journal of

Biotechnology, 15(3), 194-200.


Wong, C. F, Noor, R., Raja, Z., Rahman, A., Salleh, A. B., & Basri, M. (2011). Role

of α-Helical Structure in Organic Solvent-Activated Homodimer of Elastase

Strain K, International Journal of Molecular Sciences, 12: 5797–5814.


Wu, G. (2009). Amino acids: Metabolism, functions and nutrition. Amino Acids, 37,



Wu, G. (2010). Functional amino acids in growth, reproduction, and health. Advances

in Nutrition, 1, 31-37.


Xie, Q., Meng, F., & Zhou, H. (2004). Low Temperature Induced Conformation

Changes of Aminoacylase. Tsinghua Science and Technology, 9(1), 76–80.


Xindu, G., and Lili, W. (2008). Liquid chromatography of recombinant proteins and

protein drugs. Journal of Chromatography B, 866, 133-153.


Youshko, M.I., Rantwijk,V.F., & Sheldon, R.A. (2001). Enantioselective acylation of

chiral amines catalyzed by aminoacylase I. Tetrahedron: Asymmetr, 12,



Yusoff, N., (2007). Purification and characterization of organic solvent tolerant

protease from Pseudomonas aeruginosa strain K. (MS Thesis), Universiti

Putra Malaysia, Malaysia.


Zhao, J., Chen, Z., & Wang, Q. (2018). The Survival Mechanisms of Thermophiles at

High Temperatures : An Angle of Omics Base Biases of Thermophilic.

Physiology, 30, 97–106.


Zhou, M., & Gomez-sanchez, C. E. (2000). Universal TA Cloning. Current

Issues in Molecular Biology, 2, 1–7.


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