Isolation and characterization of new thermophilic aminoacylase from Geobacillus sp. Strain Szn

Kajian ini bertujuan untuk memencilkan dan mencirikan aminoasilase termostabildaripada bakterium termofilik. Dalam pemencilan bakterium, sampel air dan sedimen telahdiperolehi dari Air Panas Ulu Slim, Perak. Aminoasilase SZN termostabil diekstraksecara intrasellular dan ditulenkan sehingga homogen d...

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Main Author:	Suzana Adenan
Format:	thesis
Language:	eng
Published:	2018
Subjects:	QR Microbiology
Online Access:	https://ir.upsi.edu.my/detailsg.php?det=6203
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institution	Universiti Pendidikan Sultan Idris
collection	UPSI Digital Repository
language	eng
topic	QR Microbiology
spellingShingle	QR Microbiology Suzana Adenan Isolation and characterization of new thermophilic aminoacylase from Geobacillus sp. Strain Szn
description	Kajian ini bertujuan untuk memencilkan dan mencirikan aminoasilase termostabildaripada bakterium termofilik. Dalam pemencilan bakterium, sampel air dan sedimen telahdiperolehi dari Air Panas Ulu Slim, Perak. Aminoasilase SZN termostabil diekstraksecara intrasellular dan ditulenkan sehingga homogen dengan menggunakan kromatografi pertukaran ion dan pengasingan saiz dalam eksperimen seterusnya. Aminoasilase SZN yang tulen telahdicirikan pada pelbagai suhu, pH, ion logam dan perencat. Kajian struktur lebih lanjutmenggunakan spektrokopi sirkular dikroisma dilakukan bagi menentukan kestabilan a-heliks danlembaran dalam pelbagai suhu. Penghasil aminoasilase termofilik yang dipencilkan itu dikenalpasti sebagai Geobacillus sp. strain SZN. Aminoasilase SZN dicirikansebagai enzim termostabil dengan aktiviti optimum pada 60C, pH 7.5, tempoh separuhhayat 16 jam dengan peningkatan aktiviti dan kestabilan dalam beberapa ion logam danperencat 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 70C(27.6 hingga 19.5%). Sebaliknya, peratusan lembaran , telah meningkat secara stabil pada suhuyang diuji. Struktur a-heliks yang juga merupakan lokasi residu-residu pengikat logam danpemangkin yang penting, lemah sepenuhnya pada suhu melebihi 70C lalu mengakibatkan kehilanganaktiviti. Kesimpulannya, aminoasilase SZN telah dicirikan sebagai enzim termostabil berdasarkan kepada integriti struktur a-heliks dan kestabilan fungsinya pada suhutinggi. Implikasi kajian ini menunjukkan bahawa aminoasilase SZN mampu menjadi enzimaltematif kepada bioindustri berdasarkan kepada peningkatan aktiviti enzim dalam suhutinggi dan kestabilan dalam pelbagaiperencat yang diuji.
format	thesis
qualification_name
qualification_level	Master's degree
author	Suzana Adenan
author_facet	Suzana Adenan
author_sort	Suzana Adenan
title	Isolation and characterization of new thermophilic aminoacylase from Geobacillus sp. Strain Szn
title_short	Isolation and characterization of new thermophilic aminoacylase from Geobacillus sp. Strain Szn
title_full	Isolation and characterization of new thermophilic aminoacylase from Geobacillus sp. Strain Szn
title_fullStr	Isolation and characterization of new thermophilic aminoacylase from Geobacillus sp. Strain Szn
title_full_unstemmed	Isolation and characterization of new thermophilic aminoacylase from Geobacillus sp. Strain Szn
title_sort	isolation and characterization of new thermophilic aminoacylase from geobacillus sp. strain szn
granting_institution	Universiti Pendidikan Sultan Idris
granting_department	Fakulti Sains dan Matematik
publishDate	2018
url	https://ir.upsi.edu.my/detailsg.php?det=6203
_version_	1747833249052229632
spelling	oai:ir.upsi.edu.my:62032021-09-01 Isolation and characterization of new thermophilic aminoacylase from Geobacillus sp. Strain Szn 2018 Suzana Adenan QR Microbiology Kajian ini bertujuan untuk memencilkan dan mencirikan aminoasilase termostabildaripada bakterium termofilik. Dalam pemencilan bakterium, sampel air dan sedimen telahdiperolehi dari Air Panas Ulu Slim, Perak. Aminoasilase SZN termostabil diekstraksecara intrasellular dan ditulenkan sehingga homogen dengan menggunakan kromatografi pertukaran ion dan pengasingan saiz dalam eksperimen seterusnya. Aminoasilase SZN yang tulen telahdicirikan pada pelbagai suhu, pH, ion logam dan perencat. Kajian struktur lebih lanjutmenggunakan spektrokopi sirkular dikroisma dilakukan bagi menentukan kestabilan a-heliks danlembaran dalam pelbagai suhu. Penghasil aminoasilase termofilik yang dipencilkan itu dikenalpasti sebagai Geobacillus sp. strain SZN. Aminoasilase SZN dicirikansebagai enzim termostabil dengan aktiviti optimum pada 60C, pH 7.5, tempoh separuhhayat 16 jam dengan peningkatan aktiviti dan kestabilan dalam beberapa ion logam danperencat 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 70C(27.6 hingga 19.5%). Sebaliknya, peratusan lembaran , telah meningkat secara stabil pada suhuyang diuji. Struktur a-heliks yang juga merupakan lokasi residu-residu pengikat logam danpemangkin yang penting, lemah sepenuhnya pada suhu melebihi 70C lalu mengakibatkan kehilanganaktiviti. Kesimpulannya, aminoasilase SZN telah dicirikan sebagai enzim termostabil berdasarkan kepada integriti struktur a-heliks dan kestabilan fungsinya pada suhutinggi. Implikasi kajian ini menunjukkan bahawa aminoasilase SZN mampu menjadi enzimaltematif kepada bioindustri berdasarkan kepada peningkatan aktiviti enzim dalam suhutinggi dan kestabilan dalam pelbagaiperencat yang diuji. 2018 thesis https://ir.upsi.edu.my/detailsg.php?det=6203 https://ir.upsi.edu.my/detailsg.php?det=6203 text eng closedAccess Masters Universiti Pendidikan Sultan Idris Fakulti Sains dan Matematik 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 generationof protein database search programs. Nucleic Acids Research, 25, 3389-3402.Amend, J.P., Rogers, K.L., Shock, E.L., Gurrieri, S., & Inguaggiato, S. (2003)Energetics of chemolithoautotrophy in the hydrothermal system of VulcanoIsland, southern Italy. Geobiology, 1,37-58.Ash, C., Farrow, J.A.E., Wallbanks, S., & Collins, M.D. (1991). Phylogeneticheterogeneity of the genus Bacillus revealed by comparative analysis ofsmall-subunit-ribosomal RNA sequences. Letters in AppliedMicrobiology,13, 202-206.Bakker, M., Spruijt, A.S., Rantwijk, V. F. & Sheldon, R.A. (2000). Highlyenantioselective aminoacylase-catalyzed transesterification of secondaryalcohols. 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, 2,345355.Bradford, M. M., (1976). A rapid and sensitive method for the quantification ofmicrogram 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 Thermococcuslitoralis : Cloning, overexpression, characterization, and applications inbiotransformations. Extremophiles, 6(2), 111-22.Bryant, M. (2003). Biosynthesis of amino acids. Retrieved from Researchgate.comCho, H. Y., Tanizawa, K., Tanaka, H., & Soda, K. (1987). Thermostableaminoacylase from Bacillus thermoglucosidius: purification andcharacterization. Agricultural Biology Chemistry, 51, 2793- 2800.Cihan, A.C., Tekin, N., Ozcan, B., & Cokmus, C. (2012). The Genetic Diversity OfGenus Bacillus And The Related Genera Revealed by 16S rRNA GeneSequences and Ardra Analyses Isolated from Geothermal Regions ofTurkey. Brazilian Journal of Microbiology, 43(1), 309324.Curley, P., Does, C., Dreissen, A. M., Kok, J., & Sinderen, D. V. (2003). Purificationand characterisation of a lactococcal aminoacylase. ArchieveMicrobiology, 179, 402-408.Deleage G., & Geourjon. C. (1995). SOPMA: significant improvements in proteinsecondary structure prediction by concensus prediction from multipleallignments. Computer Applications in the Biosciences, 11(6), 681-684.Derekova, A., Mandeva, R., & Kambourova, M. (2008). Phylogenetic diversity ofthermophilic carbohydrate degrading bacilli from Bulgarian hot springs.World Journal of Microbiology and Biotechnology, 24, 1697-1702.Faraldos, J., Arroyo, E., & Herradn, B. (1997). Biocatalysis in organic synthesis.Highly enantioselective kinetic resolution of secondary alcohols catalyzedby 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 andanalysis. Nucleic Acids Research, 31, 3784-3788.Greenfield, N. J. (2009). Using circular dichroism spectra to estimate proteinsecondary structure. Nature Protocols, 1(6), 28762890.Handbook of Proteolytic Enzymes. (1998). London: Academic Press.Hickey, D.A., & Singer, G.A. (2004). Genomic and proteomic adaptations to growthat high temperature. Genome Biology 5, (117), 1-117.Holt, K. (2004). Biocatalysis and chemocatalysis - a powerful combination for thepreparation of enantiomerically pure -amino acids. Pharmachem 3, 24.Hsu, C., Lai, W., Chang, W., & Liaw, S. (2002). Structural-based mutational analysisof D -aminoacylase from Alcaligenes faecalis DA1, Protein Science, 11,25452550.Huffer, S., Clark, M.E., Ning, J.C., Blanch, H.W., & Clark, D.S. (2011). The Role ofAlcohols in Growth, Lipid Composition, and Membrane Fluidity of Yeast,Bacteria, and Archaea. Applied and Environmental Microbiology. 77(18),64006408.Hurst, L.D., & Merchant, A.R. (2001). High guanine-cytosine content is not anadaptation to high temperature: a comparative analysis amongstprokaryotes. Proceedings. Biological sciences Royal Society, 268, (1466),493.Ishikawa, K., Ishida, H., Matsui, I., Kawarabayasi, Y., & Kikuchi, H. (2001). Novelbifunction hyperthermostable carboxypeptidase/aminoacylase fromPyrococcus horikoshii OT3. Applied and Environmental Microbiology, 67,673-679.Ivanov, K., Stoimenova, A., Obreshkova, D., & Saso, L. (2014). Biotechnology in theProduction 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 novelalkaline protease from Bacillus horikoshii. Journalof Microbiology and Biotechnology, 22(1), 5868.Jozic, D., Bourenkow, G., Bartunik, H., Scholze, H., Dive, V., Henrich, et al (2002).Crystal structure of the dinuclear zinc aminopeptidase PepV fromLactobacillus delbrueckii unravels its preference for dipeptides. Structure, 10(8), 10971106.Kokkinidis, B. M., Glykos, N. M., & Fadouloglou, V. E. (2012). Chapter 7 - ProteinFlexibility and Enzymatic Catalysis. Advances in Protein Chemistry andStructural Biology, 87: 181-218.Koreishi, M., Asayama, F., Imanaka, H., Imamura, K., Kadota, M., Tsuno, T., &Nakanishi, K. (2005). Purification and characterization of a novelaminoacylase from Streptomyces mobaraensis. Bioscience, Biotechnology,and Biochemistry, 69(10), 19141922.Koreishi, M., Nakatani, Y., Ooi, M., Imanaka, H., Imamura, K., & Nakanishi, K.(2009). Purification , Characterization , Molecular Cloning , and Expression ofa New Aminoacylase from Streptomyces mobaraensis That Can HydrolyzeN - (Middle / Long) -chain-fatty-acyl-L-amino Acids as Well as N -Shortchain-acyl-L-amino acids. Bioscience, Biotechnology, and Biochemistry, 73(9), 19401947.Kramers, H.A. (1940). Brownian motion in a field of force and the diffusion model ofchemical reactions. Physica, 7,284304.Kumar, S., & Nussinov, R. (1999). Salt bridge stability in monomeric proteins.Journal of Molecular Biology, 293, 12411255.Kumar, S., Stecher, G., & Tamura, K. (2016). MEGA7 : Molecular EvolutionaryGenetics Analysis version 7.0 for bigger datasets MEGA7. MolecularBiology and Evolution, 33(7),18701874.Kyte, J., & Doolittle, R. F. (1982). A simple method for displaying the hydropathiccharacter of protein. Journal of Molecular Biology,157, 105-132.Liljeblad, A., Aksela, R., and Kanerva, L.T. (2001). Use of enantio-, chemo- andregioselectivity 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/carboxypeptidasefrom radioresistant bacterium Deninococcus radiodurans R1. Journal ofBiotechnology, 128, 322-334.Lindner, H. A., Lunin, V. V, Alary, A., Hecker, R., & Cygler, M. (2003). EssentialRoles of Zinc Ligation and Enzyme Dimerization for Catalysis in theAminoacylase-1 /M20 Family. Journal of Biological Chemistry, 278(45),4449644504.Littlechild, J. A. (2015). Enzymes from extreme environments and their industrialapplications. Process and Industrial Biotechnology, 3(161), 19.Logan, N.A., Berge, O., Bishop, A,H., Busse, H.J., de Vos, P. et al (2009). Proposedminimal standards for describing new taxa of aerobic, endospore- formingbacteria. International Journal of Systematic and Evolutionary Microbiology,59, 21142121.Ludwig, W., Schleifer, K.H., & Whitman, W.B. (2007). Revised road map to thephylum Firmicutes. Bergeys Manual Trust websitehttp://www.bergeys.org/outlines/Bergeys.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 evidencethat the intracellular proteins of archaeal microbes contain disulfidebonds. Proceedings of the National Academy of Sciences,99, 96799684.Marguet, E., & Forterre, P. (1998). Protection of DNA by salts againstthermodegradation at temperatures typical for hyperthermophiles.Extremophiles, 2, 115-122.Martnez-rodrguez, S., Garca-pino, A., Las, J., Clemente-jimnez, J. M., Rodrguezvico,F., Garca-ruiz, J. et al (2012). Mutational and Structural Analysis of L -N -Carbamoylase Reveals New Insights into a Peptidase M20 / M25 / M40Family Member. Journal of Bacteriology,194 (21), 57595768.McKee, T., & McKee, J. R., (2003). Enzymes. In: Biochemistry: The molecularbasis 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.Miana-Galbis, D., Pinzn, D.L., Lorn, 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 EvolutionaryMicrobiology, 60, 1600-1604.Minasov, G., Shuvalova, L., Brunzelle, J.S., Collart, F.R., Anderson, W.F., &Midwest (unpublished). Crystal Structure of Bacillus Subtilis YXEPProtein (APC1829), a Dinuclear Metal Binding Peptidase from M20Family Center for Structural Genomics (MCSG).Moore, S. & Stein, W.H. (1948). Photometric Ninhydrin Method for Use in TheChromatography of Amino Acids. Journal of Biological Chemistry, 176, 367-388.Muiz-Lozano, F., Domnguez-Snchez, G. & Daz-Viveros, Y. (1998). DAminoacylasefrom a novel producer: Stenotrophomonas maltophilia ITV-059521: 296. The Journal of Industrial Microbiology and Biotechnology, 21(6), 296299.Nakagawa, S., & Takai, K. (2006). The isolation of thermophiles from deep-seahydrothermal 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). pHDependentConformational Changes in Proteins and Their Effect onExperimental pK a s : The Case of Nitrophorin. PLOS Computational Biology,8(11).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 Geobacillusuzenensis sp. nov. from petroleum reservoirs and transfer of Bacillusstearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans,Bacillus kaustophilus, Bacillus thermoglucosidius and Bacillusthermodenitrificans to Geobacillus as the new combinations G.stearothermophilus, G. thermocatenulatus, G. thermoleovorans,G.kaustophilus, G. thermoglucosidasius and G.thermodenitrificans. InternationalJournal of Systematic Evolutionary Microbiology, 51, 433-446.Otieno, D. O. (2010). Synthesis of -Galactooligosaccharides from Lactose UsingMicrobial Galactosidases. Food Science & Technology, 9, 471482.Pace, N.R. 1997. L- and D- Amino Acids The biology place. Science, 276, 734740.Retrieved from http://www.phschool.com/science/biology_place/biocoach/bioprop/landd.html : Pearson EducationParker B. M., Taylor I. N., Woodley J. M., Ward J. M. & Dalby P.A. (2011). Directedevolution of a thermostable l-aminoacylase biocatalyst. Journal ofBiotechnology, 155 (4), 396-405.Patel, R. N. (2013). Biocatalytic Synthesis of Chiral Alcohols and Amino Acids forDevelopment of Pharmaceuticals. Biomolecules,3, 741777.Petersen, T.N., Brunak, S., von Heijne, G.,& Nielsen, H. (2011). SignalP 4.0:discriminating signal peptides from transmembrane regions. Nature Methods,8(10),785-6.Rainey, F.A., Fritze, D., & Stackebrandt, E. (1994). The phylogenetic diversity ofthermophilic members of the genus Bacillus as revealed by 16S rRNAanalysis. FEMS Microbiology Letters,115, 205-211.Raja Noor Zaleha Rahman Raja Abdul Rahman, Geok, Mahiran Basri, & Abu BakarSalleh, (2006). An organic solvent-stable alkaline protease from Pseudomonasaeruginosa strain K: Enzyme purification and characterization. Enzyme andMicrobial Technology. 39,1484-1491Rampelotto, P. H. (2010). Resistance of Microorganisms to Extreme EnvironmentalConditions and Its Contribution to Astrobiology. Sustainability, 2, 1602-1623.Raussens, V., Ruysschaert, J.M., & Goormaghtigh, E. (2003). Protein concentration isnot an absolute prerequisite for the determination of secondary structure fromcircular dichroism spectra: a new scaling method. Analytical Biochemistry,114-21.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 analkaline serine protease from sea water haloalkaliphilic bacterium. Annals ofMicrobiology. 65(1), 371381.Rawlings, N.D., Morton, F.R., Kok, C.Y., Kong, J., & Barrett, A.J. (2008). MEROPS:the peptidase database. Nucleic Acids Research,36, 320325.Razvi, A., & Scholtz, J. M. (2006). Lessons in stability from thermophilic proteins.Protein Science, 15,15691578.Researchnester.com. (2018). Amino Acids Market : Global Demand Analysis &Opportunity Outlook 2024. Retrieved fromhttps://www.researchnester.com/reports amino-acids-market-global-demandanalysis-opportunity-outlook-2024/424.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 MarketSize, Share, Trends, Global Industry Report, 2022. Retrieved fromhttps://www.grandviewresearch.com/industry-analysis/amino-acids-market.Robinson, P. K. (2015). Enzymes : principles and biotechnological applications,Essays Biochem. (2015) 59, 141.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 methoda new method forreconstructing phylogenetic trees. Molecular Biology and Evolution, 4,406425.Sakanyan, V., Desmarez, L., Legrain, C., Charlier, D., Mett, I., & Kochikyan, A. et al(1993). Gene cloning, sequence analysis, purification, and characterization ofa thermostable aminoacylase from Bacillus strearothermophilus. Applied andEnvironmental Microbiology, 59, 3878-3888.Schiraldi, C., Giuliano, M., & Rosa, M. D. E. (2002). Perspectives onbiotechnological applications of archaea. Archaea, 1, 7586.Shock, E.L., McCollom, T., & Schulte, M.D. (1998). Thermophiles: the Keys toMolecular Evolution and the Origin of Life. 5976.Stetter, K. O. (1996). Hyperthermophile Prokaryotes. FEMS Microbiology Reviews,18,149-158.Story, S. V., Grunden, A. M., & Adams, M. W. (2001). Characterization of anaminoacylase from the hyperthermophilic archaeon Pyrococcusfuriosus. Journal of Bacteriology, 183, 4259-4268.Subramaniam, S. (1998). The Biology Workbench: a seamless database and analysisenvironment for the biologist. Proteins, 32, 1-2.Tamura, K., Nei, M., & Kumar, S. (2004). Prospects for inferring very largephylogenies by using the neighborjoining method. Proceedings of theNational Academy of Sciences (USA) 101,11030-11035.Tanimoto, K., Higashi, N., Nishioka, M., Ishikawa, K., & Taya, M. (2008).Characterization of thermostable aminoacylase from hyperthermophilicarchaeon Pyrococcus horikoshii, Federation of European BiochemicalSocieties Journal , 275, 11401149.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 biotransformationprocesses. Biochemical Society Transactions, 32(2).Ulrih, N.P., Gmajner, D., & Raspor, P. (2009). Structural and physico- chemicalproperties of polar lipids from thermophilic archaea. Applications ofMicrobiologyand Biotechnolology, 84,249260.Unsworth, L. D., Oost, J. Van Der, & Koutsopoulos, S. (2007). Hyperthermophilicenzymes stability, activity and implementation strategies for hightemperature applications. Federation of European Biochemical Societies, 274,40444056.Uribe, S., & Sampedro, J. G. (2003). Measuring Solution Viscosity and its Effect onEnzyme Activity. Biological Procedures Online, 5(1),108115. Vieille, C., &Zeikus, G. J., (2001). Hyperthermophilic Enzymes: Sources Uses and MolecularMechanisms for Thermostability Hyperthermophilic Enzymes: Sources, Uses,and Molecular Mechanisms for Thermostability. Microbiology and MolecularBiology Reviews, 65(1),143.Vieille, C., Burdette, D. S., & Zeikus, J. G. (1996). Thermozymes. BiotechnologyAnnual Report, 2,183.Vieille, C., Zeikus, G. J., & Vieille, C. (2001). Hyperthermophilic Enzymes : SourcesUses and Molecular Mechanisms for Thermostability. Microbiology andMolecular Biology Reviews, 65(1): 143.Wardenga, R., Lindner, H. A., Hollmann, F., Thum, O., & Bornscheuer, U. (2010).Biochimie Increasing the synthesis / hydrolysis ratio of aminoacylase 1 bysite-directed mutagenesis. Biochimie, 92(1), 102109.Wei, H. M., Palm, G. J., & Rohm, K. (1995). Thermostable Aminoacylase fromBacillus stearothermophilus : Significance of the Metal Center for Catalysisand Protein Stability. Biological chemistry Hoppe-Seyler, 376, 643649.Wong, C. F, Noor, R., Raja, Z., Rahman, A., Salleh, A. B., & Basri, M. (2017).Construction of New Genetic Tools as Alternatives for Protein Overexpressionin Escherichia coli and Pseudomonas aeruginosa. Iranian Journal ofBiotechnology, 15(3), 194-200.Wong, C. F, Noor, R., Raja, Z., Rahman, A., Salleh, A. B., & Basri, M. (2011). Roleof -Helical Structure in Organic Solvent-Activated Homodimer of ElastaseStrain K, International Journal of Molecular Sciences, 12: 57975814.Wu, G. (2009). Amino acids: Metabolism, functions and nutrition. Amino Acids, 37,1-17.Wu, G. (2010). Functional amino acids in growth, reproduction, and health. Advancesin Nutrition, 1, 31-37.Xie, Q., Meng, F., & Zhou, H. (2004). Low Temperature Induced ConformationChanges of Aminoacylase. Tsinghua Science and Technology, 9(1), 7680.Xindu, G., and Lili, W. (2008). Liquid chromatography of recombinant proteins andprotein drugs. Journal of Chromatography B, 866, 133-153.Youshko, M.I., Rantwijk,V.F., & Sheldon, R.A. (2001). Enantioselective acylation ofchiral amines catalyzed by aminoacylase I. Tetrahedron: Asymmetr, 12,3267-3271.Yusoff, N., (2007). Purification and characterization of organic solvent tolerantprotease from Pseudomonas aeruginosa strain K. (MS Thesis), UniversitiPutra Malaysia, Malaysia.Zhao, J., Chen, Z., & Wang, Q. (2018). The Survival Mechanisms of Thermophiles atHigh Temperatures : An Angle of Omics Base Biases of Thermophilic.Physiology, 30, 97106.Zhou, M., & Gomez-sanchez, C. E. (2000). Universal TA Cloning. CurrentIssues in Molecular Biology, 2, 17.

Isolation and characterization of new thermophilic aminoacylase from Geobacillus sp. Strain Szn

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