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Role of Anionic Polysaccharide (Alginate) on Activity, Stability and Recycling Efficiency of Bacterial Endo (1→4) β-d-Glucanase of GH12 Family

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Abstract

Extracellular partially purified endo (1→4) β-d-glucanase belong to CAZy Family GH12 produced by Bacillus licheniformis KIBGE-IB2 was immobilized within the microenvironment of calcium alginate beads using entrapment technique. Immobilization technology is one of the supporting technique for obtaining purified product with cost effectiveness. The activities of soluble and immobilized endo (1→4) β-d-glucanase were compared using carboxymethyl cellulose (CMC) as a substrate. The results showed that the maximum immobilization of enzyme was achieved when calcium chloride (0.2 M) and sodium alginate (2.0%) were used. The pH optima of soluble and immobilized enzyme remain same, but temperature optima (60 °C) of entrapped enzyme shifted to a higher level (70 °C) as compared to soluble enzyme. The scanning electron microscopy analysis reveals the changes in morphology and size of micro pores on the surface of calcium alginate before and after immobilization. The immobilized enzyme showed its reusability up to five cycles. The stability against various inhibitors was also improved after immobilization.

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References

  1. Lynd LR, Weimer PJ, Van Zyl WH, Pretorius IS (2002) Microbial cellulose utilization: fundamentals and biotechnology. Microbiol Mol Bio Rev 66:506–577

    Article  CAS  Google Scholar 

  2. Bhat MK (2000) Cellulases and related enzymes in biotechnology. Biotech Advant 18:355–383

    Article  CAS  Google Scholar 

  3. Sukumaran RK, Singhania RR, Pandey A (2005) Microbial cellulases-production, applications and challenges. J Sci Ind Res 64:832–844

    CAS  Google Scholar 

  4. Ahmed S, Bashir A, Saleem H, Saadia M, Jamil A (2009) Production and purification of cellulose-degrading enzymes from a filamentous fungus Trichoderma harzianum. Pak J Bot 41:1411–1419

    CAS  Google Scholar 

  5. Karmakar M, Ray RR (2011) Current trends in research and application of microbial cellulases. Res J Microbiol 6:41–53

    Article  CAS  Google Scholar 

  6. Eshafai AM, Haroun BM, Hassan MM, Fatah OM, Atta HM, Othman AM (2009) Properties of extracellular carboxymethyl cellulase produced by Aspergillus terreus DSM 826 using some agricultural wastes. J Genet Eng Biotech 6:29–36

    Google Scholar 

  7. Juwaied AA, Al Amiery ABH, Abdumuniem Z, Anaam U (2011) Optimization of cellulase production by Aspergillus niger and Tricoderma viride using sugar cane waste. J Yeast Fungal Res 2:19–23

    CAS  Google Scholar 

  8. Drevon GF, Danielmeier K, Federspiel W, Stolz DB, Wicks DA, Yu PC, Russell AJ (2002) High-activity enzyme-polyurethane coatings. Biotechnol Bioeng 79:785–794

    Article  CAS  Google Scholar 

  9. Sarrouh B, Santos TM, Miyoshi A, Dias R, Azevedo V (2012) Up-to-date insight on industrial enzymes applications and global market. J Bioprocess Biotechniq S 4:002 doi:10.4172/2155-9821.S4-002.

    Google Scholar 

  10. Karim A, Nawaz MA, Aman A, Ul Qader SA (2015) Hyper production of cellulose degrading endo (1,4) β-d-glucanase from Bacillus licheniformis KIBGE-IB2. J Rad Res Appl Sci 8:160–165

    Google Scholar 

  11. Konsoula Z, Liakopoulou-Kyriakides M (2006) Thermostable α-amylase production by Bacillus subtilis entrapped in calcium alginate gel capsules. Enzyme Microb Technol 39:690–696

    Article  CAS  Google Scholar 

  12. Smidsrød O (1990) Alginate as immobilization matrix for cells. Trends Biotechnol 8:71–78

    Article  Google Scholar 

  13. Rehman HU, Aman A, Silipo A, Qader SAU, Molinaro A, Ansari A (2013) Degradation of complex carbohydrate: immobilization of pectinase from Bacillus licheniformis KIBGE-IB21 using calcium alginate as a support. Food Chem 139:1081–1086

    Article  Google Scholar 

  14. Tekedar HC (2009) Molecular cloning overexpression and characterization of thermostable esterase and lipase from Thermophilic Bacillus sp. (Thesis)

  15. Andriani D, Sunwoo C, Ryu HW, Prasetya B, Park DH (2012) Immobilization of cellulase from newly isolated strain Bacillus subtilis TD6 using calcium alginate as a support material. Bioproc Biosyst Eng 35:29–33

    Article  CAS  Google Scholar 

  16. Norouzian D (2003) Enzyme immobilization, and the state of art in biotechnology: a review. Iran J Biotechnol 1:197–206

    CAS  Google Scholar 

  17. Sungur S, Akbulut U (1994) Immobilization of beta-galactosidase onto gelatin by glutaraldehyde and chromium(III) acetate. J Chem Technol Biotechnol 59:303–306

    Article  CAS  Google Scholar 

  18. Huang XL, Walsh MK, Swaisgood HE (1996) Simultaneous isolation and immobilization of streptavidin-beta-galactosidase-some kinetic characteristics of the immobilized enzyme and regeneration of bioreactors. Enzyme Microbial Technol 19:378–383

    Article  CAS  Google Scholar 

  19. Ates S, Mehmetoglu UA (1997) New method for immobilization of beta-galactosidase and its utilization in a plug flow reactor. Process Biochem 32:433–436

    Article  CAS  Google Scholar 

  20. Faiza S, Aman A, Nawaz MA, Karim A, Qader SAU (2017) Chitosan hydrogel microspheres: an effective covalent matrix for crosslinking of soluble dextranase to increase stability and recycling efficiency. Bioprocess Biosyst Eng. doi:10.1007/s00449-016-1713-7

    Google Scholar 

  21. Riaz A, Qader SAU, Anwar A, Iqbal S (2009) Immobilization of a thermostable A-amylase on calcium alginate beads from Bacillus subtilis KIBGE-HAR. Aust J Basic Appl Sci 3:2883–2887

    CAS  Google Scholar 

  22. Shafiei M, Ziaee AA, Amoozegar MA (2011) Purification and characterization of an organic-solvent-tolerant halophilic alpha-amylase from the moderately halophilic Nesterenkonia sp. strain F. J Ind Microbiol Biotechnol 38:275–281

    Article  CAS  Google Scholar 

  23. Lei Z, Bi S (2007) The silica-coated chitosan particle from a layer-by-layer approach for pectinase immobilization. Enzyme Microb Tech 40:1442–1447

    Article  CAS  Google Scholar 

  24. Sartoglu K, Demir N, Acar J, Mutlu M (2001) The use of commercial pectinase in the fruit industry, part 2: determination of kinetic behavior of immobilized commercial pectinase. J Food Eng 47:271–274

    Article  Google Scholar 

  25. Buga ML, Ibrahim S, Nok AJ (2010) Physico-chemical characteristics of immobilized polygalacturonase from Aspergillus niger (SA6). Afr J Biotechnol 9:8934–8943

    CAS  Google Scholar 

  26. Karim A, Qader SAU, Nazwaz A, Aman A (2014) Immobilization of endo (1→4) β-d-glucanase from Bacillus licheniformis KIBGE-IB2 using agar–agar as support for continuous use. Chem Eng Trans 38:409–414

    Google Scholar 

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Correspondence to Shah Ali Ul Qader.

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Karim, A., Nawaz, M.A., Aman, A. et al. Role of Anionic Polysaccharide (Alginate) on Activity, Stability and Recycling Efficiency of Bacterial Endo (1→4) β-d-Glucanase of GH12 Family. Catal Lett 147, 1792–1801 (2017). https://doi.org/10.1007/s10562-017-2074-9

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  • DOI: https://doi.org/10.1007/s10562-017-2074-9

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