Indian Journal of Microbiology

, Volume 59, Issue 4, pp 401–409 | Cite as

Synthetic Biology Perspectives of Microbial Enzymes and Their Innovative Applications

  • Pratyoosh ShuklaEmail author
Review article


Microbial enzymes are high in demand and there is focus on their efficient, cost effective and eco-friendly production. The relevant microbial enzymes for respective industries needs to be identified but the conventional technologies don’t have much edge over it. So, there is more attention towards high throughput methods for production of efficient enzymes. The enzymes produced by microbes need to be modified to bear the extreme conditions of the industries in order to get prolific outcomes and here the synthetic biology tools may be augmented to modify such microbes and enzymes. These tools are applied to synthesize novel and efficient enzymes. Use of computational tools for enzyme modification has provided new avenues for faster and specific modification of enzymes in a shorter time period. This review focuses on few important enzymes and their modification through synthetic biology tools including genetic modification, nanotechnology, post translational modification.


Microbial enzymes Nanotechnology Synthetic biology Enzyme modification 



The author acknowledges the help by Mr. Mandeep for the formatting of the manuscript. PS acknowledges the Department of Microbiology, Barkatullah University, Bhopal, India for their infrastructural support for D.Sc. Work. The infrastructural support from Department of Science and Technology, New Delhi, Govt. of India, through FIST Grant (Grant No. 1196 SR/FST/LS-I/2017/4) and Department of Biotechnology, Government of India (Grant No. BT/PR27437/BCE/8/1433/2018) is duly acknowledged.


  1. 1.
    Kumar V, Dangi AK, Shukla P (2018) Engineering thermostable microbial xylanases toward its industrial applications. Mol Biotechnol 60:226–235. CrossRefPubMedGoogle Scholar
  2. 2.
    Han H, Ling Z, Khan A, Virk AK, Kulshrestha S, Li X (2019) Improvements of thermophilic enzymes: from genetic modifications to applications. Bioresour Technol 279:350–361. CrossRefPubMedGoogle Scholar
  3. 3.
    Böttcher D, Bornscheuer UT (2010) Protein engineering of microbial enzymes. Curr Opin Microbiol 13:274–282. CrossRefPubMedGoogle Scholar
  4. 4.
    Yang H, Li J, Du G, Liu L (2017) Microbial production and molecular engineering of industrial enzymes: challenges and strategies. In: Biotechnology of microbial enzymes. Academic Press, Cambridge, pp 151–165. CrossRefGoogle Scholar
  5. 5.
    Liu ZQ, Lu MM, Zhang XH, Cheng F, Xu JM, Xue YP, Jin LQ, Wang YS, Zheng YG (2018) Significant improvement of the nitrilase activity by semi-rational protein engineering and its application in the production of iminodiacetic acid. Int J Biol Macromol 116:563–571. CrossRefPubMedGoogle Scholar
  6. 6.
    Srivastava N, Srivastava M, Ramteke PW, Mishra PK (2019) Synthetic biology strategy for microbial cellulases: an overview. In: New and future developments in microbial biotechnology and bioengineering. Elsevier, Amsterdam, pp 229–238. CrossRefGoogle Scholar
  7. 7.
    Liu M, Dai X, Guan R, Xu X (2014) Immobilization of Aspergillus niger xylanase A on Fe3O4-coated chitosan magnetic nanoparticles for xylooligosaccharide preparation. Catal Commun 55:6–10. CrossRefGoogle Scholar
  8. 8.
    Patel SK, Kalia VC, Choi JH, Haw JR, Kim IW, Lee JK (2014) Immobilization of laccase on SiO2 nanocarriers improves its stability and reusability. J Microbiol Biotechnol 24:639–647. CrossRefPubMedGoogle Scholar
  9. 9.
    Mostafa FA, El Aty AAA (2018) Thermodynamics enhancement of Alternaria tenuissima KM651985 laccase by covalent coupling to polysaccharides and its applications. Int J Biol Macromol 120:222–229. CrossRefPubMedGoogle Scholar
  10. 10.
    Pandi A, Kuppuswami GM, Ramudu KN, Palanivel S (2019) A sustainable approach for degradation of leather dyes by a new fungal laccase. J Clean Prod 211:590–597. CrossRefGoogle Scholar
  11. 11.
    Xu G, Wang J, Yin Q, Fang W, Xiao Y, Fang Z (2019) Expression of a thermo-and alkali-philic fungal laccase in Pichia pastoris and its application. Protein Expr Purif 154:16–24. CrossRefPubMedGoogle Scholar
  12. 12.
    Ranimol G, Venugopal T, Gopalakrishnan S, Sunkar S (2018) Production of laccase from Trichoderma harzianum and its application in dye decolourisation. Biocatal Agric Biotechnol 16:400–404. CrossRefGoogle Scholar
  13. 13.
    Cardoso BK, Linde GA, Colauto NB, do Valle JS (2018) Panus strigellus laccase decolorizes anthraquinone, azo, and triphenylmethane dyes. Biocatal Agric Biotechnol 16:558–563. CrossRefGoogle Scholar
  14. 14.
    Ellaiah P, Prabhakar T, Ramakrishna B, Taleb AT, Adinarayana K (2004) Production of lipase by immobilized cells of Aspergillus niger. Process Biochem 39:525–528. CrossRefGoogle Scholar
  15. 15.
    Abada EA (2019) Application of microbial enzymes in the dairy industry. In: Enzymes in food biotechnology. Academic Press, Cambridge, pp 61–72. CrossRefGoogle Scholar
  16. 16.
    Suriya J, Bharathiraja S, Krishnan M, Manivasagan P, Kim SK (2016) Marine microbial amylases: properties and applications. In: Advances in food and nutrition research. Academic Press, Cambridge, vol 79, pp 161–177. CrossRefGoogle Scholar
  17. 17.
    Wang J, Li Y, Lu F (2018) Molecular cloning and biochemical characterization of an α-amylase family from Aspergillus niger. Electr J Biotechnol 32:55–62. CrossRefGoogle Scholar
  18. 18.
    Roy JK, Borah A, Mahanta CL, Mukherjee AK (2013) Cloning and overexpression of raw starch digesting α-amylase gene from Bacillus subtilis strain AS01a in Escherichia coli and application of the purified recombinant α-amylase (AmyBS-I) in raw starch digestion and baking industry. J Mol Catal B Enzym 97:118–129. CrossRefGoogle Scholar
  19. 19.
    Bach E, Sant’Anna V, Daroit DJ, Corrêa APF, Segalin J, Brandelli A (2012) Production, one-step purification, and characterization of a keratinolytic protease from Serratia marcescens P3. Process Biochem 47:2455–2462. CrossRefGoogle Scholar
  20. 20.
    Yu XC, Ma SL, Xu Y, Fu CH, Jiang CY, Zhou CY (2017) Construction and application of a novel genetically engineered Aspergillus oryzae for expressing proteases. Electr J Biotechnol 29:32–38. CrossRefGoogle Scholar
  21. 21.
    Lakshmi BKM, Kumar DM, Hemalatha KPJ (2018) Purification and characterization of alkaline protease with novel properties from Bacillus cereus strain S8. J Genet Eng Biotechnol 16:295–304. CrossRefPubMedPubMedCentralGoogle Scholar
  22. 22.
    Sudha S, Nandhini SU, Mathumathi V, Nayaki JMA (2018) Production, optimization and partial purification of protease from terrestrial bacterium Exiguobacterium profundam sp. MM1. Biocatal Agric Biotechnol 16:347–352. CrossRefGoogle Scholar
  23. 23.
    Dos Santos Aguilar JG, Sato HH (2018) Microbial proteases: production and application in obtaining protein hydrolysates. Food Res Int 103:253–262. CrossRefPubMedGoogle Scholar
  24. 24.
    Mechri S, Kriaa M, Berrouina MBE, Benmrad MO, Jaouadi NZ, Rekik H, Bouacem K, Bouanane-Darenfed A, Chebbi A, Sayadi S, Chamkha M (2017) Optimized production and characterization of a detergent-stable protease from Lysinibacillus fusiformis C250R. Int J Biol Macromol 101:383–397. CrossRefPubMedGoogle Scholar
  25. 25.
    Souza PM, Werneck G, Aliakbarian B, Siqueira F, Ferreira Filho EX, Perego P, Junior AP (2017) Production, purification and characterization of an aspartic protease from Aspergillus foetidus. Food Chem Toxicol 109:1103–1110. CrossRefPubMedGoogle Scholar
  26. 26.
    Da Silva OS, de Almeida EM, de Melo AHF, Porto TS (2018) Purification and characterization of a novel extracellular serine-protease with collagenolytic activity from Aspergillus tamarii URM4634. Int J Biol Macromol 117:1081–1088. CrossRefPubMedGoogle Scholar
  27. 27.
    Lim L, Senba H, Kimura Y, Yokota S, Doi M, Yoshida KI, Takenaka S (2018) Influences of N-linked glycosylation on the biochemical properties of aspartic protease from Aspergillus glaucus MA0196. Process Biochem 79:74–80. CrossRefGoogle Scholar
  28. 28.
    Pascoal A, Estevinho LM, Martins IM, Choupina AB (2018) Novel sources and functions of microbial lipases and their role in the infection mechanisms. Physiol Mol Plant Pathol 104:119–126. CrossRefGoogle Scholar
  29. 29.
    Cihangir N, Sarikaya E (2004) Investigation of lipase production by a new isolate of Aspergillus sp. World J Microbiol Biotechnol 20:193–197. CrossRefGoogle Scholar
  30. 30.
    Singh AK, Mukhopadhyay M (2012) Overview of fungal lipase: a review. Appl Biochem Biotechnol 166:486–520. CrossRefPubMedGoogle Scholar
  31. 31.
    Nigam VK, Arfi T, Kumar V, Shukla P (2017) Bioengineering of nitrilases towards its use as green catalyst: applications and perspectives. Indian J Microbiol 57:131–138. CrossRefPubMedPubMedCentralGoogle Scholar
  32. 32.
    Xu Z, Cai T, Xiong N, Zou SP, Xue YP, Zheng YG (2018) Engineering the residues on “A” surface and C-terminal region to improve thermostability of nitrilase. Enzyme Microb Technol 113:52–58. CrossRefPubMedGoogle Scholar
  33. 33.
    Chen H, Chen Z, Ni Z, Tian R, Zhang T, Jia J, Yang S (2016) Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner. J Mol Catal B Enzym 123:73–80. CrossRefGoogle Scholar
  34. 34.
    Holyavka MG, Kayumov AR, Baydamshina DR, Koroleva VA, Trizna EY, Trushin MV, Artyukhov VG (2018) Efficient fructose production from plant extracts by immobilized inulinases from Kluyveromyces marxianus and Helianthus tuberosus. Int J Biol Macromol 115:829–834. CrossRefPubMedGoogle Scholar
  35. 35.
    Singh RS, Chauhan K, Kennedy JF (2017) A panorama of bacterial inulinases: production, purification, characterization and industrial applications. Int J Biol Macromol 96:312–322. CrossRefPubMedGoogle Scholar
  36. 36.
    Singh RS, Chauhan K, Kennedy JF (2019) Fructose production from inulin using fungal inulinase immobilized on 3-aminopropyl-triethoxysilane functionalized multiwalled carbon nanotubes. Int J Biol Macromol 125:41–52. CrossRefPubMedGoogle Scholar
  37. 37.
    Singh RS, Chauhan K (2017) Inulinase production from a new inulinase producer, Penicillium oxalicum BGPUP-4. Biocatal Agric Biotechnol 9:1–10. CrossRefGoogle Scholar
  38. 38.
    Markham KA, Alper HS (2018) Synthetic biology expands the industrial potential of Yarrowia lipolytica. Trends Biotechnol 36:1085–1095. CrossRefPubMedGoogle Scholar
  39. 39.
    Kumar P, Patel SK, Lee JK, Kalia VC (2013) Extending the limits of Bacillus for novel biotechnological applications. Biotechnol Adv 31:1543–1561. CrossRefPubMedPubMedCentralGoogle Scholar
  40. 40.
    Singh D, Rawat S, Waseem M, Gupta S, Lynn A, Nitin M, Sharma KK (2016) Molecular modeling and simulation studies of recombinant laccase from Yersinia enterocolitica suggests significant role in the biotransformation of non-steroidal anti-inflammatory drugs. Biochem Biophys Res Commun 469:306–312. CrossRefPubMedGoogle Scholar
  41. 41.
    Sahnoun M, Jemli S, Trabelsi S, Bejar S (2018) Modifing Aspergillus oryzae S2 amylase substrate specificity and thermostability through its tetramerisation using biochemical and in silico studies and stabilization. Int J Biol Macromol 117:483–492. CrossRefPubMedGoogle Scholar
  42. 42.
    Lončar N, Božić N, Lopez-Santin J, Vujčić Z (2013) Bacillus amyloliquefaciens laccase–from soil bacteria to recombinant enzyme for wastewater decolorization. Bioresour Technol 147:177–183. CrossRefPubMedGoogle Scholar
  43. 43.
    Deep K, Poddar A, Das SK (2016) Cloning, overexpression, and characterization of halostable, solvent-tolerant novel β-endoglucanase from a marine bacterium photobacterium panuliri LBS5 T (DSM 27646 T). Appl Biochem Biotechnol 178:695–709. CrossRefPubMedGoogle Scholar
  44. 44.
    Gainza-Cirauqui P, Correia BE (2018) Computational protein design—the next generation tool to expand synthetic biology applications. Curr Opin Biotechnol 52:145–152. CrossRefPubMedGoogle Scholar
  45. 45.
    Purohit HJ, Tikariha H, Kalia VC (2018) Current scenario on application of computational tools in biological systems. In: Soft computing for biological systems. Springer, Singapore, pp 1–12. CrossRefGoogle Scholar
  46. 46.
    McCarty NS, Ledesma-Amaro R (2018) Synthetic biology tools to engineer microbial communities for biotechnology. Trends Biotechnol 37:181–197. CrossRefPubMedGoogle Scholar
  47. 47.
    Kuzuwa S, Yokoi KJ, Kondo M, Kimoto H, Yamakawa A, Taketo A, Kodaira KI (2012) Properties of the inulinase gene levH1 of Lactobacillus casei IAM 1045; cloning, mutational and biochemical characterization. Gene 495:154–162. CrossRefPubMedGoogle Scholar
  48. 48.
    Garuba EO, Onilude A (2018) Immobilization of thermostable exo-inulinase from mutant thermophilic Aspergillus tamarii-U4 using kaolin clay and its application in inulin hydrolysis. J Genet Eng Biotechnol 16:341–346. CrossRefPubMedPubMedCentralGoogle Scholar
  49. 49.
    Emtenani S, Asoodeh A, Emtenani S (2015) Gene cloning and characterization of a thermostable organic-tolerant α-amylase from Bacillus subtilis DR8806. Int J Biol Macromol 72:290–298. CrossRefPubMedGoogle Scholar
  50. 50.
    Li D, Park JT, Li X, Kim S, Lee S, Shim JH, Park SH, Cha J, Lee BH, Kim JW, Park KH (2010) Overexpression and characterization of an extremely thermo-stable maltogenic amylase, with an optimal temperature of 100 °C, from the hyperthermophilic archaeon Staphylothermus marinus. N Biotechnol 27:300–307. CrossRefPubMedGoogle Scholar
  51. 51.
    Karam EA, Wahab WAA, Saleh SA, Hassan ME, Kansoh AL, Esawy MA (2017) Production, immobilization and thermodynamic studies of free and immobilized Aspergillus awamori amylase. Int J Biol Macromol 102:694–703. CrossRefPubMedGoogle Scholar
  52. 52.
    Li S, Yang Q, Tang B, Chen A (2018) Improvement of enzymatic properties of Rhizopus oryzae α-amylase by site-saturation mutagenesis of histidine 286. Enzyme Microbiol Technol 117:96–102. CrossRefGoogle Scholar
  53. 53.
    Johnson J, Yang YH, Lee DG, Yoon JJ, Choi KY (2018) Expression, purification and characterization of halophilic protease Pph_Pro1 cloned from Pseudoalteromonas phenolica. Protein Expres Purif 152:46–55. CrossRefGoogle Scholar
  54. 54.
    Sun H, Wang H, Gao W, Chen L, Wu K, Wei D (2015) Directed evolution of nitrilase PpL19 from Pseudomonas psychrotolerans L19 and identification of enantiocomplementary mutants toward mandelonitrile. Biochem Biophys Res Commun 468:820–825. CrossRefPubMedGoogle Scholar
  55. 55.
    Mueller P, Egorova K, Vorgias CE, Boutou E, Trauthwein H, Verseck S, Antranikian G (2006) Cloning, overexpression, and characterization of a thermoactive nitrilase from the hyperthermophilic archaeon Pyrococcus abyssi. Protein Expres Purif 47:672–681. CrossRefGoogle Scholar
  56. 56.
    Acevedo JP, Reetz MT, Asenjo JA, Parra LP (2017) One-step combined focused epPCR and saturation mutagenesis for thermostability evolution of a new cold-active xylanase. Enyzme Microbiol Technol 100:60–70. CrossRefGoogle Scholar
  57. 57.
    bin Abdul Wahab MKH, bin Jonet MA, Illias RM (2016) Thermostability enhancement of xylanase Aspergillus fumigatus RT-1. J Mol Catal B Enzym 134:154–163. CrossRefGoogle Scholar
  58. 58.
    Tang F, Chen D, Yu B, Luo Y, Zheng P, Mao X, He J (2017) Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds. Electr J Biotechnol 26:52–59. CrossRefGoogle Scholar
  59. 59.
    de Souza AR, de Araújo GC, Zanphorlin LM, Ruller R, Franco FC, Torres FA, Mertens JA, Bowman MJ, Gomes E, Da Silva R (2016) Engineering increased thermostability in the GH-10 endo-1,4-β-xylanase from Thermoascus aurantiacus CBMAI 756. Int J Biol Macromol 93A:20–26. CrossRefGoogle Scholar
  60. 60.
    Joshi R, Sharma R, Kuila A (2019) Lipase production from Fusarium incarnatum KU377454 and its immobilization using Fe3O4 NPs for application in waste cooking oil degradation. Bioresour Technol Rep 5:134–140. CrossRefGoogle Scholar
  61. 61.
    Prabaningtyas RK, Putri DN, Utami TS, Hermansyah H (2018) Production of immobilized extracellular lipase from Aspergillus niger by solid state fermentation method using palm kernel cake, soybean meal, and coir pith as the substrate. Energy Procedia 153:242–247. CrossRefGoogle Scholar
  62. 62.
    Jayawardena MB, Yee LH, Poljak A, Cavicchioli R, Kjelleberg SJ, Siddiqui KS (2017) Enhancement of lipase stability and productivity through chemical modification and its application to latex-based polymer emulsions. Process Biochem 57:131–140. CrossRefGoogle Scholar
  63. 63.
    El-Batal AI, ElKenawy NM, Yassin AS, Amin MA (2015) Laccase production by Pleurotus ostreatus and its application in synthesis of gold nanoparticles. Biotechnol Rep 5:31–39. CrossRefGoogle Scholar
  64. 64.
    Wen X, Du C, Wan J, Zeng G, Huang D, Yin L, Zhang J (2019) Immobilizing laccase on kaolinite and its application in treatment of malachite green effluent with the coexistence of Cd (П). Chemosphere 217:843–850. CrossRefPubMedGoogle Scholar
  65. 65.
    Vite-Vallejo O, Palomares LA, Dantán-González E, Ayala-Castro HG, Martínez-Anaya C, Valderrama B, Folch-Mallol J (2009) The role of N-glycosylation on the enzymatic activity of a Pycnoporus sanguineus laccase. Enzyme Microb Technol 45:233–239. CrossRefGoogle Scholar
  66. 66.
    Kumar V, Kumar A, Chhabra D, Shukla P (2019) Improved biobleaching of mixed hardwood pulp and process optimization using novel GA-ANN and GA-ANFIS hybrid statistical tools. Bioresour Technol 271:274–282. CrossRefPubMedGoogle Scholar
  67. 67.
    Clark DP, Pazdernik NJ, McGehee MR (2019). Chapter 7—Cloning genes for synthetic biology. In: Molecular biology, 3rd edn, pp 199–239. CrossRefGoogle Scholar
  68. 68.
    Shrivastava S, Shukla P, Deepalakshmi PD, Mukhopadhyay K (2013) Characterization, cloning and functional expression of novel xylanase from Thermomyces lanuginosus SS-8 isolated from self-heating plant wreckage material. World J Microbiol Biotechnol 29:2407–2415. CrossRefPubMedGoogle Scholar
  69. 69.
    Yang JK, Zhang JW, Mao L, You X, Chen GJ (2016) Genetic modification and optimization of endo-inulinase for the enzymatic production of oligofructose from inulin. J Mol Catal B Enzym 134:225–232. CrossRefGoogle Scholar
  70. 70.
    Xu X, Qi LS (2018) A CRISPR-dCas toolbox for genetic engineering and synthetic biology. J Mol Biol 431:34–47. CrossRefPubMedGoogle Scholar
  71. 71.
    Miao C, Yang L, Wang Z, Luo W, Li H, Lv P, Yuan Z (2018) Lipase immobilization on amino-silane modified superparamagnetic Fe3O4 nanoparticles as biocatalyst for biodiesel production. Fuel 224:774–782. CrossRefGoogle Scholar
  72. 72.
    Diyanat S, Homaei A, Mosaddegh E (2018) Immobilization of Penaeus vannamei protease on ZnO nanoparticles for long-term use. Int J Biol Macromol 118:92–98. CrossRefPubMedGoogle Scholar
  73. 73.
    Singh PK, Joseph J, Goyal S, Grover A, Shukla P (2016) Functional analysis of the binding model of microbial inulinases using docking and molecular dynamics simulation. J Mol Model 22:69. CrossRefPubMedGoogle Scholar
  74. 74.
    Karthik MVK, Shukla P (2012) Computational strategies towards improved protein function prophecy and in silico structure based mutagenesis of xylanases from Thermomyces Lanuginosus. Springer, Berlin. CrossRefGoogle Scholar
  75. 75.
    Shrivastava S, Shukla P, Poddar H (2007) In silico studies for evaluating conservation homology among family 11 xylanases from Thermomyces lanuginosus. J Appl Sci Environ Sanit 2:70–76Google Scholar
  76. 76.
    Shrivastava S, Kumar V, Baweja M, Shukla P (2016) Enhanced xylanase production from Thermomyces lanuginosus NCIM 1374/DSM 28966 using statistical analysis. J Pure Appl Microbiol 10:2225–2231Google Scholar
  77. 77.
    Holyavka MG, Kondratyev MS, Samchenko AA, Kabanov AV, Komarov VM, Artyukhov VG (2016) In silico design of high-affinity ligands for the immobilization of inulinase. Comput Biol Med 71:198–204. CrossRefPubMedGoogle Scholar
  78. 78.
    Ryšlavá H, Doubnerova V, Kavan D, Vaněk O (2013) Effect of posttranslational modifications on enzyme function and assembly. J Proteom 92:80–109. CrossRefGoogle Scholar
  79. 79.
    Bond AE, Row PE, Dudley E (2011) Post-translation modification of proteins; methodologies and applications in plant sciences. Phytochemistry 72:975–996. CrossRefPubMedGoogle Scholar
  80. 80.
    Cain JA, Solis N, Cordwell SJ (2014) Beyond gene expression: the impact of protein post-translational modifications in bacteria. J Proteom 97:265–286. CrossRefGoogle Scholar
  81. 81.
    Janusz G, Jaszek M, Matuszewska A, DrĿczkowski P, Osiſska-Jaroszuk M (2015) Proteolytic modifications of laccase from Cerrena unicolor. J Mol Catal B Enzym 122:330–338. CrossRefGoogle Scholar
  82. 82.
    Bao C, Zhang Q (2019) Modulation of protein activity and assembled structure by polymer conjugation: PEGylation vs glycosylation. Eur Polym J 112:263–272. CrossRefGoogle Scholar
  83. 83.
    Kumar V, Marin-Navarro J, Shukla P (2016) Thermostable microbial xylanases for pulp and paper industries: trends, applications and further perspectives. World J Microbiol Biotechnol 32:34. CrossRefPubMedGoogle Scholar
  84. 84.
    Baweja M, Nain L, Kawarabayasi Y, Shukla P (2016) Current technological improvements in enzymes toward their biotechnological applications. Front Microbiol 7:965. CrossRefPubMedPubMedCentralGoogle Scholar
  85. 85.
    Gupta SK, Shukla P (2018) Glycosylation control technologies for recombinant therapeutic proteins. Appl Microbiol Biotechnol 102:10457–10468. CrossRefPubMedGoogle Scholar
  86. 86.
    Kumar V, Shukla P (2018) Extracellular xylanase production from T. lanuginosus VAPS24 at pilot scale and thermostability enhancement by immobilization. Process Biochem 71:53–60. CrossRefGoogle Scholar
  87. 87.
    Kumar V, Singh PK, Shukla P (2018) Thermostability and substrate specificity of GH-11 Xylanase from Thermomyces lanuginosus VAPS24. Indian J Microbiol 58:515–519. CrossRefPubMedGoogle Scholar
  88. 88.
    Basu M, Kumar V, Shukla P (2018) Recombinant approaches for microbial xylanases: recent advances and perspectives. Curr Protein Pept Sci 19:87–99. CrossRefPubMedGoogle Scholar
  89. 89.
    Kumar V, Baweja M, Liu H, Shukla P (2017) Microbial enzyme engineering: applications and perspectives. In: Recent advances in applied microbiology. Springer, Singapore, pp 259–273. CrossRefGoogle Scholar
  90. 90.
    Sinha R, Shukla P (2019) Current trends in protein engineering: updates and progress. Curr Protein Pept Sci 20:398–407. CrossRefPubMedGoogle Scholar

Copyright information

© Association of Microbiologists of India 2019

Authors and Affiliations

  1. 1.Enzyme Technology and Protein Bioinformatics Laboratory, Department of MicrobiologyMaharshi Dayanand UniversityRohtakIndia

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