home icon user icon
Welcome to International Network for Natural Sciences | INNS Pub.
Home My Account
Submit Manuscript
double_slash
breadcumb_bg

Thermal stability of two xylanases from Macrotermes subhyalinus little soldier: kinetic and thermodynamic analysis

Paper Details

Research Paper 01/01/2018
Views (439) Download (23)
current_issue_feature_image
publication_file

Thermal stability of two xylanases from Macrotermes subhyalinus little soldier: kinetic and thermodynamic analysis

Jean Bedel Fagbohoun, Mankambou Jacques Gnanwa, Detto Karamoko Bi Eugene Toma Zan, Soumaila Dabonne, Lucien Patrice Kouame
Int. J. Biosci.12( 1), 65-75, January 2018.
Certificate: IJB 2018 [Generate Certificate]
Key: Kinetic parametersMacrotermes subhyalinusThermodynamic parametersXylanases

Abstract

The knowledge on thermal inactivation kinetics of enzymes is necessary to allow their adequate utilization as natural biopreservatives in the food industry and technology applications. In this work, the kinetics of thermal inactivation was studied for the previously purified and characterized xylanases Xyl1 and Xyl2 from Macrotermes subhyalinus little soldier. Samples of xylanases were treated at different time-temperature combinations in the range of 5-60 min at 50-65°C and the kinetic and thermodynamic parameters for xylanases were calculated. The inactivation kinetic follows a first-order reaction with k-values between 0.0192 ± 0.0002 to 0.0405 ± 0.0003 and 0.0119 ± 0.0005 to 0.0418 ± 0.0004 min-1 for Xyl1 and Xyl2, respectively. Activation energy (Ea) and Z-values were estimated to 48.08 ± 1.84 kJ mol-1 and 43.47 ± 3.02°C for Xyl1, 75.52 ± 3.52 kJ.mol-1 and 27.77 ± 1.87°C for Xyl2. The catalytic reactions of both xylanases are endothermic due to positive enthalpy. The high value obtained for the variation in enthalpy of activation indicates that a high amount of energy is required to initiate denaturation, probably due to the molecular conformation of xylanases. All results suggest that both xylanases are relatively resistant to long heat treatments up to 50°C.

VIEWS 26
Cover PDF

Anema SG, McKenna AB. 1996. Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk. Journal of Agricultural and Food Chemistry 44(2), p. 422-428. http://dx.doi.org/10.1016/j.biortech.2006.02.036

Arogba SS, Ajiboye OL, Ugboko LA, Essienette SY, Afolabi PO. 1998. Properties of polyphenol oxidase in mango (Mangifera indica) kernel. Journal of the Science of Food and Agriculture 77(4), p. 459-462. www,doi.org/10.1002/(SICI)10970010(199808)77:4

Awuah GB, Ramaswamy HS, Economides A. 2007. Thermal processing and quality: Principles and overview. Chemical Engineering Process 46, 584-602. http://dx.doi.org/10.1016/j.cep.2006.08.004

Bajaj BK, Manhas K. 2012. Production and characterization of xylanase from Bacillus licheniformis P 11 (C) with potential for fruit juice and bakery industry. Biocatalyst Agriculture and Biotechnology 1(4), 330-337.

Bankeeree W, Lotrakul P, Prasongsuk S, Chaiareekij S, Eveleigh DE, Kim SW, Hunsa Punnapayak. 2014. Effect of polyols on thermostability of xylanase from a tropical isolate of Aureobasidium pullulans and its application in prebleaching of rice straw pulp. Springer Open Journal. 3:37.

Bhatti HN, Batool  S, Afzal  N. 2013.  Production and characterization    of    a    novel    beta-glucosidase    from Fusarium solani. International Journal of Agriculture and Biology 15, 140‒144.

Bhatti HN, Zia A, Nawaz R, Sheikh MA, Rashid MH, Khalid AM. 2005. Effect of   copper ions on thermal stability of glucoamylase from Fusarium sp. International Journal of Agriculture and Biology 7(4), 585-587.

Bromberg A, Marx S, Frishman G. 2008. Kinetic study of the thermalinactivation of cholinesterase enzymes immobilized in solid matrices. Biochimical and Biophysical Acta, 1784(6), 961-966 p. http://dx.doi.org/10.1016/j.bbapap.2008.02.018

Cui L, Du G, Zhang D, Chen J. 2008. Thermal stability and conformational changes of transglutaminase from a newly isolated Streptomyces hygroscopicus. Bio. Resources 99:3794 – 3800.

D’Amico S, Marx JC, Gerday C, Feller G. 2003. Activity-stability relationships in extremophilic enzymes. The Journal of Biological Chemistry, 278(10), p. 7891-7896. https://doi.org/10.1074/jbc.M212508200

De Meneres  CR,  Silva  IS,  Pavarina  EC,  deFaria  AF,  Franciscon  E, Durrant  LR. 2010.  Production  of  xylooligosccharides from enzymatic  hydrolysis  of  xylan  by  white-rot  fungi  Pleurotus. Acta Science and Technology 32(1), 37-42.

Dhiman SS, Garg G, Sharma J, Mahajan R, Methoxy. 2011. Characterization of statistically produced xylanase for enrichment of fruit juice clarification process, New Biotechnology 2(6), 746-755.

Dogan M, Arslan O, Dogan S. 2002. Substrate specificity, heat inactivation and inhibition of polyphenol oxidase from different aubergine cultivars. International Journal of Food Science and Technology 37(4), p. 415-423. https://doi.org/10.1046/j.1365-2621.2002.00580.x

Driss D, Driss Z, Chaari F, Chaabouni, SE. 2014. Immobilization of His-tagged recombinant xylanase from Penicillium occitanis on Nickel-chelate Eupergit C for increasing digestibility of poultry feed. Bioengineered Landes Bioscience 5(4), 274–279. http://dx.doi.org/10.1007/s.12010-014-0932-0

Espachs-Barroso A, Loey AV, Hendrickx, M, Martín-Belloso O. 2006. Inactivation of plant pectin methylesteraseby thermal or high intensity pulsed electric field treatments. Innovative Food Science and Emerging Technologies 7, 40–48. http://dx.doi.org/10.1016/j.ifset.2005.07.002

Fagbohoun JB. 2013. Propriétés biochimiques, analyses cinétique et thermodynamique des enzymes responsables de la cellulolyse et de la xylanolyse chez le petit soldat du termite Macrotermes subhyalinus (Termitidae, Macrotermitinae). Ph.D. Thesis, Université Nangui Abrogoua, Abidjan, Côte d’Ivoire.

Fagbohoun JB, Ahi AP, Karamoko Y, Dabonné S,  Kouadio EJP, Kouamé  LP. 2012. An endo-beta-D-glycosidase from salivary glands of Macrotermes subhyalinus  little  soldier  with  a  dual activity   against   carboxymethylcellulose   and   xylan. International Journal of Biosciences 2, 1-10.

 Fu D, Li C, Lu J, Rahman A, Tan T. 2010. Relationship between thermal inactivation and conformational change of Yarrowia lipolytica lipase and the effect of additives on enzyme stability. Journal of Molecule Catalysis B-Enzymatic 66, 136 – 141.

Georis J, Esteves F, de L, Lamotte-Brasseur J, Bougnet V, Devreese B, Giannotta F, Granier B, Frere JM. 2000. An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: structural basis and molecular study. Protein Science, 9(3), p. 466-475. https://doi.org/10.1110/ps.9.3.466

Guiavarc’h YP, Deli V, Van Loey AM, Hendrickx ME. 2002. Development of anenzymic time temperature integrator forsterilization processes based on Bacillus licheniformis alpha-amylase at reduced water content. Journal of Food Science, 67(1), p. 285-291. https://doi.org/10.1111/j.1365-2621.2002.tb11399.x

Gummadi SN. 2003. What is the role of thermodynamics in protein stability? Biotechnology Bioprocess Engineery 8, 9 – 18.

Lappe R, Cladera-Olivera F, Domingue APM, Brandelli A. 2009. Kinetics and thermodynamics of thermal inactivation of the antimicrobial peptide cerein 8A.Journal of Food Engineering, 91, 223–227. http://dx.doi.org/10.1016/j.jfoodeng.2008.08.025

Leite RSR, Gomes E, da Silva R. 2007. Characterization and comparison of thermostability of purified β-glucosidases from a mesophilic Aureobasidium pullulans and a thermophilic Thermoascusaur antiacus. Process Biochemistry, 42(7), 1101-1106. http://dx.doi.org/10.1016/j.procbio.2007.05.003

Li X, Li E, Zhu Y, Teng C, Sun B, Song H, Yang R. 2012. A typical endo xylanase from Streptomyces rameus L. 2001 and its unique characteristics in xylo oligosaccharide production. Carbohydrates Resources 359(10), 30-36.

Lopes AM, Valeri D, Pessoa-Júnior A. 2013. Comparison of kinetic characteristics of xylanases from Aspergillus niger and Trichoderma sp. with pH and temperature baking process parameters. African Journal of Biotechnology  12(19), 2640-2645 p.

Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. 1951. Protein measurement with thefolin phenol reagent. Journal of Biological Chemistry, 193, p. 265-275.

Marangoni AG. 2002. Characterization of Enzyme Stability, in Enzyme Kinetics: A Modern Approach. John Wiley & Sons, Inc., Hoboken, NJ, USA. https://doi.org/10.1002/0471267295.ch12

Marin E, Sanchez L, Perez MD, Puyol P, Calvo M. 2003. Effect of heat treatment on bovine lactoperoxidase activity in skim milk: kinetic and thermodynamic analysis. Journal of Food and Science 68(1), 89-93. https://doi.org/10.1111/j.1365-2621.2003.tb14120.x

Nagar S, Mittal A, Kumar D, Kumar L, Gupta VK. 2012. Immobilization of xylanase on glutaraldehyde activated aluminium oxide pellets for increasing digestibility of poultry feed. Process Biochemistry 47(9), 1402-1410.

Ninawe S, Kapoor M, Kuhad RC. 2008. Purification and characterization of extracellular xylanase from Streptomyces cyaneus SN32. Bioresource Technology 99(5), 1252-1258 p. http://dx.doi.org/10.1016/j.biortech.2007.02.016

Pal A, Khanum F. 2010. Characterizing and improving the thermostability of purified xylanase from Aspergillus niger DFR-5 grown on solid-state-medium. Journal of Biochemistry and Technology 2, 203 – 209.

Qiu Z, Shi P, Luo H, Bai Y, Yuan T, Yang P, Liu S, Yao BA. 2010. xylanase with broad pH and temperature adaptability from Streptomyces megaspores DSM. 41476, and its potential application in brewing industry. Enzymology Microbiology and Technology 46(6), 506-512.

Riaz H, Jabbar A, Rashid MH, Riaz S, Latif F. 2014. Endoglucanase production by Humicola insolens: effect of physiochemical factors on growth kinetics and thermodynamics. International Journal Of Agriculture and Biology, 16(6), 1141-146 p.

Romdhane BIB, Achouri IM, Belghith H. 2010. Improvement of highly thermostable  xylanases production by Talaromyces thermophilus for the agro-industrials residue hydrolysis. Applied Biochemistry and Biotechnology, vol. 162(6), p. 1635-1646.

Sant’Anna V, Utpott M, Cladera-Olivera F,  Brandelli A. 2011. Influence of pH and  sodium  chloride  on  kinetics  of  thermal  inactivation  of  bacteriocin-like substance P34. Journal of Applied Microbiology 110, 156–162. https://doi.org/10.1111/j.1365-2672.2010.04868.x

SarathBabu VR, Kumar MA, Karanth NG,  Thakur MS. 2004.  Stabilization of  immobilized  glucose  oxidase  against  thermal inactivation  by  silanization  for  biosensor  applications. Biosen Bioelectron 19, 1337-134. http://dx.doi.org/10.1016/j.bios.2003.11.024

Shallom D, Shoham Y. 2003. Microbial hemicellulases. Current Opinion on  Microbiology 6, 219-228.

Singh S, Pillay B, Prior BA. 2000. Thermal stability of β-xylanases produced by  different  Thermomyces lanuginosus  strains.  Enzymology Microbiology and Technology 26, 502-508.

Srivastava R, Brown JK, Zhu H, McShane MJ. 2005. Stabilization of glucose oxidase in alginate microspheres with photo reactive diazoresin nanofilm coatings. Biotechnology and Bioengineering 91, 124-131. https://doi.org/10.1002/bit.20469

Sriyapai T, Somyoonsap P, Matsui K, Kawai, F, Chansiri K. 2011. Cloning of a thermostable xylanase from Actinomadura sp. S14 and its expression in Escherichia coli and Pichia pastoris. Journal of Bioscience and Bioengineering, 111(5), p. 528-536.

Stauffer CE. 1989. Enzyme assays for food scientists (1st Ed.). New York: Van Nostr and Reinhold, p. 67-78.

Stumbo CR. 1973. Thermobacteriology in food processing (2nd Ed.). New York: Academic Press, p. 336.

Tayefi-Nasrabadi H, Asadpour R. 2008. Effect of heat treatment on buffalo (Bubalus bubalis) lactoperoxidase activity in raw milk. Journal of Biology Science 8(8), 1310-1315. https://doi.org/10.3923/jbs.2008.1310.1315

Trasar-Cepeda C, Gil-Sotres F, Leiro´S, MC. 2007. Thermodynamic parameters of enzymes in grassland soils from Galicia, NW Spain. Soil Biologyand Biochemistry 39(1), 311-319 p. http://dx.doi.org/10.1016/j.soilbio.2006.08.002

Van Boekel MAJS. 2008. Kinetic modelling of food quality: A critical review. Comprehensive Reviews in Food Science and Food Safety, 7(1), 144-158 p. https://doi.org/10.1111/j.1541-4337.2007.00036.x

Vieille C, Zeikus JG. 1996. Thermozymes: identifying molecular determinants of protein structural and functional stability. Trends in Biotechnology, 14(6), p. 183-190. http://dx.doi.org/10.1016/0167-7799(96)10026-3

Viikari L, Alapuranen M, Puranen T, Vehmaanperä J, Siika-aho M. 2007. Thermostable enzymes in lignocellulose hydrolysis. Adv Biochemistry Eng and Biotechnology108, 121 – 145.

Ya KC, Konan KH, Gnangui SN, Kouamé LP. 2014. Study of thermal stability of beta-glucosidase from the land crab digestive juice (Cardisoma armatum): kinetic and thermodynamic analysis. International Journal of Development Research 4, 1836-1840 p.

Yaws CL. 1999. Chemical properties handbook: physical thermodynamic, environmental, transport, safety and health related properties for organic and inorganic chemicals; McGraw-Hill:  New York, NY.

Submit Manuscript