An overview on preparation of enzymes for industrial use

References

• Aberer W, Hahn M, Klade M, Seebacher U, Spök A, Wallner K, Witzani H. 2002. Final report: collection of information on enzymes. Brussels, Belgium: European Commission. European Commission Contract No (Vol. 2). B4-3040/2000/27845/MAR.
   Google Scholar
• Akdis CA. 2021. Does the epithelial barrier hypothesis explain the increase in allergy, autoimmunity and other chronic conditions? Nat Rev Immunol. 21(11):739–751. doi: 10.1038/s41577-021-00538-7.
   PubMed Web of Science ®Google Scholar
• Amin N, Liu AD, Ramer S, Aehle W, Meijer D, Metin M, Wong S, Gualfetti P, Schellenberger V. 2004. Construction of stabilized proteins by combinatorial consensus mutagenesis. Protein Eng Des Sel. 17(11):787–793. doi: 10.1093/protein/gzh091.
   PubMed Web of Science ®Google Scholar
• Angkawinitwong U, Sharma G, Khaw PT, Brocchini S, Williams GR. 2015. Solid-state protein formulations. Ther Deliv. 6(1):59–82. doi: 10.4155/tde.14.98.
   PubMedGoogle Scholar
• Arbige MV, Pitcher WH. 1989. Industrial enzymology: a look towards the future. Trends Biotechnol. 7(12):330–335. doi: 10.1016/0167-7799(89)90032-2.
   Web of Science ®Google Scholar
• Back JF, Oakenfull D, Smith MB. 1979. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry. 18(23):5191–5196. doi: 10.1021/bi00590a025.
   PubMed Web of Science ®Google Scholar
• Bairoch A. 2000. The ENZYME database in 2000. Nucleic Acids Res. 28(1):304–305. doi: 10.1093/nar/28.1.304.
   PubMed Web of Science ®Google Scholar
• Balcão VM, Vila MM. 2015. Structural and functional stabilization of protein entities: state-of-the-art. Adv Drug Deliv Rev. 93:25–41. doi: 10.1016/j.addr.2014.10.005.
   PubMed Web of Science ®Google Scholar
• Becker T, Park G, Gaertner AL. 1997. Formulation of detergent enzymes. Enzymes in detergency Boca Raton (FL): CRC Press; p. 299–326.
   Google Scholar
• Bhatt HB, Singh SP. 2020. Cloning, expression, and structural elucidation of a biotechnologically potential alkaline serine protease from a newly isolated haloalkaliphilic Bacillus lehensis JO-26. Front Microbiol. 11:941. doi: 10.3389/fmicb.2020.00941.
   PubMed Web of Science ®Google Scholar
• Bosquillon C, Rouxhet PG, Ahimou F, Simon D, Culot C, Préat V, Vanbever R. 2004. Aerosolization properties, surface composition and physical state of spray-dried protein powders. J Control Release. 99(3):357–367. doi: 10.1016/j.jconrel.2004.07.022.
   PubMed Web of Science ®Google Scholar
• Brahmachari G. 2016. Biotechnology of microbial enzymes: production, biocatalysis and Industrial applications. Amsterdam, Netherlands: Academic Press, Elsevier; p. 280.
   Google Scholar
• Brzozowski AM, Lawson DM, Turkenburg JP, Bisgaard-Frantzen H, Svendsen A, Borchert TV, Dauter Z, Wilson KS, Davies GJ. 2000. Structural analysis of a chimeric bacterial α-amylase: high-resolution analysis of native and ligand complexes. Biochemistry. 39(31):9099–9107. doi: 10.1021/bi0000317.
   PubMed Web of Science ®Google Scholar
• Buchholz K, Bornscheuer UT. 2017. Enzyme technology: history and current trends. Applied bioengineering: innovations and future directions. Hoboken (NJ): Wiley; p. 13–46.
   Google Scholar
• Chaplin MF, Bucke C. 1990. Enzyme technology. New York (NY): Cambridge University Press Archive; p. 73.
   Google Scholar
• Chen K, Arnold FH. 2020. Engineering new catalytic activities in enzymes. Nat Catal. 3(3):203–213. doi: 10.1038/s41929-019-0385-5.
   Web of Science ®Google Scholar
• Clarke KG. 2013. Downstream processing. Bioprocess engineering: an introductory engineering and life science approach. Amsterdam, Netherlands: Elsevier; p. 209–234.
   Google Scholar
• Dale D, Becker T, Reichman M, Maurer S. 2022. Delivery and stabilization of e\\nzymes. Enzymes in farm animal nutrition. Wallingford: CABI; p. 207–219.
   Google Scholar
• Delplancke PFA, Braeckman KG. 2017. Liquid detergent composition. Procter and Gamble Co, U.S. Patent Application 15/334,634.
   Google Scholar
• DeSantis G, Jones JB. 1999. Chemical modification of enzymes for enhanced functionality. Curr Opin Biotechnol. 10(4):324–330. doi: 10.1016/S0958-1669(99)80059-7.
   PubMed Web of Science ®Google Scholar
• Estell DA, Wells JA. 1988. Modified enzymes and methods for making same. Genencor Inc, U.S. Patent 4,760,025.
   Google Scholar
• FAO/WHO. 2019. Safety evaluation of certain food additives. Eighty fourth meeting. Geneva, Switzerland: FAO/WHO.
   Google Scholar
• FAO/WHO. 2002. Expert committee on food additives. Fifty ninth meeting. Geneva, Switzerland: FAO/WHO.
   Google Scholar
• FAO/WHO. 2007. General specifications and considerations for enzyme preparations used in food processing. Evaluation of certain food additives and contaminants. Sixty-seventh meeting. Geneva, Switzerland: FAO/WHO.
   Google Scholar
• Fernandes DA, Costa E, Leandro P, Corvo ML. 2022. Formulation of spray dried enzymes for dry powder inhalers: an integrated methodology. Int J Pharm. 615:121492. doi: 10.1016/j.ijpharm.2022.121492.
   PubMedGoogle Scholar
• Figard P. 1951. Glycerol fermentation of starch. Lowa State Collage J Sci. 25:208–210. doi: 10.31274/rtd-180813-14707
   Google Scholar
• Galanakis CM. 2021. Functionality of Food Components and Emerging Technologies. Foods. 10(1):128. doi: 10.3390/foods10010128.
   PubMed Web of Science ®Google Scholar
• Guerrero-Navarro AE, Ríos-Castillo AG, Ripolles-Avila C, Zamora A, Hascoët AS, Felipe X, Castillo M, Rodríguez-Jerez JJ. 2022. Effectiveness of enzymatic treatment for reducing dairy fouling at pilot-plant scale under real cleaning conditions. LWT-Food Sci Technol. 154:112634. doi: 10.1016/j.lwt.2021.112634.
   Web of Science ®Google Scholar
• Herrera-Márquez O, Fernández-Serrano M, Pilamala M, Jácome MB, Luzón G. 2019. Stability studies of an amylase and a protease for cleaning processes in the food industry. Food Bioprod Process. 117:64–73. doi: 10.1016/j.fbp.2019.06.015.
   Web of Science ®Google Scholar
• IUB. 1961. Report of the commission on enzymes of the international union of biochemistry. IUB aymposium series. Vol. 20. New York (NY): Pergamon Press.
   Google Scholar
• Jordan S, Katz JS, Yezer B, Derjaguin LVO. 2021. Excipients: characterization, purpose, and selection. Protein instability at interfaces during drug product development: fundamental understanding, evaluation, and mitigation. Berlin, Germany: Springer; p. 249–269.
   Google Scholar
• Jørgensen JT, Jacobsen C, Hansen KU, Jørgensen A, Oftelund D, Bach P, Søndergaard GB. 2005. Spray dried enzyme product. Novozymes AS, U.S. Patent 6,924,133.
   Google Scholar
• Ju J, Li Z, Wei W, Simonsen O, Andersen KB, Du W. 2020. Encapsulated solid enzyme product, Novozymes. US patent 20200087597 A1.
   Google Scholar
• Juturu V, Wu JC. 2014. Microbial cellulases: engineering, production and applications. Renew Sust Energ Rev. 33:188–203. doi: 10.1016/j.rser.2014.01.077.
   Web of Science ®Google Scholar
• Kamini NR, Hemachander C, Mala JGS, Puvanakrishnan R. 1999. Microbial enzyme technology as an alternative to conventional chemicals in leather industry. Curr Sci. 77(1):80–86. https://www.jstor.org/stable/24102916
   Web of Science ®Google Scholar
• Kazlauskas R. 2018. Engineering more stable proteins. Chem Soc Rev. 47(24):9026–9045. doi: 10.1039/c8cs00014j.
   PubMed Web of Science ®Google Scholar
• Khambhaty Y. 2020. Applications of enzymes in leather processing. Environ Chem Lett. 18(3):747–769. doi: 10.1007/s10311-020-00971-5.
   Web of Science ®Google Scholar
• Kralova I, Sjöblom J. 2009. Surfactants used in food industry: a review. J Dispers Sci Technol. 30(9):363–1383. doi: 10.1080/01932690902735561
   Web of Science ®Google Scholar
• Kumar A, Singh S. 2013. Directed evolution: tailoring biocatalysts for industrial applications. Crit Rev Biotechnol. 33(4):365–378. doi: 10.3109/07388551.2012.716810.
   PubMed Web of Science ®Google Scholar
• Li J, Krause ME, Tu R. 2021. Overview of the impact of protein interfacial instability on the development of biologic products. Protein instability at interfaces during drug product development. Berlin, Germany: Springer; p. 1–8.
   Google Scholar
• Linderstrom-Lang K. 1937. Enzymes. Annu Rev Biochem. 6(1):43–72. doi: 10.1146/annurev.bi.06.070137.000355.
   Google Scholar
• Ma J, Hou X, Gao D, Lv B, Zhang J. 2014. Greener approach to efficient leather soaking process: role of enzymes and their synergistic effect. J Clean Prod. 78:226–232. doi: 10.1016/j.jclepro.2014.04.058.
   Web of Science ®Google Scholar
• Madhu A, Chakraborty JN. 2017. Developments in application of enzymes for textile processing. J Clean Prod. 145:114–133. doi: 10.1016/j.jclepro.2017.01.013.
   Web of Science ®Google Scholar
• Martinez R, Jakob F, Tu R, Siegert P, Maurer KH, Schwaneberg U. 2013. Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution. Biotechnol Bioeng. 110(3):711–720. doi: 10.1002/bit.24766.
   PubMed Web of Science ®Google Scholar
• Mensink MA, Frijlink HW, Van Der Voort Maarschalk K, Hinrichs WL. 2017. How sugars protect proteins in the solid state and during drying (review): mechanisms of stabilization in relation to stress conditions. Eur J Pharm Biopharm. 114:288–295. doi: 10.1016/j.ejpb.2017.01.024.
   PubMed Web of Science ®Google Scholar
• Mojsov KD. 2016. Aspergillus enzymes for food industries. New and future developments in microbial biotechnology and bioengineering. Amsterdam, Netherlands: Elsevier; p. 215–222.
   Google Scholar
• Mojsov K. 2014. Biopolishing enzymes and their applications in textiles: a review. Tekstilna Industrija. 61(2):20–24. https://eprints.ugd.edu.mk/id/eprint/12966
   Google Scholar
• Mondal S, Mondal K, Halder SK, Thakur N, Mondal KC. 2022. Microbial Amylase: old but still at the forefront of all major industrial enzymes. Biocatal Agric Biotechnol. 45:102509. doi: 10.1016/j.bcab.2022.102509.
   Web of Science ®Google Scholar
• Mozhaev VV, Melik-Nubarov NS, Sergeeva MV, Šikšnis V, Martinek K. 1990. Strategy for stabilizing enzymes part one: increasing stability of enzymes via their multi-point interaction with a support. Biocatalysis. 3(3):179–187. doi: 10.3109/10242429008992060.
   Google Scholar
• Niyonzima FN, Veena SM, More SS. 2020. Industrial production and optimization of microbial enzymes. Microbial enzymes: roles and applications in industries. Berlin, Germany: Springer; p. 115–135.
   Google Scholar
• Northrop JH. 1929. Crystalline pepsin. Science. 69(1796):580–580. doi: 10.1126/science.69.1796.580.
   PubMedGoogle Scholar
• Novozymes-new enzyme makes high protein drinks taste better. 2021. https://www.novozymes.com/en/news/news-archive/2021/1/new-enzyme-makes-high-protein-drinks-taste-better.
   Google Scholar
• Nunes CS, Philipps-Wiemann P. 2018. Formulation of enzymes. Enzymes in human and animal nutrition. Amsterdam, Netherlands: Academic Press, Elsevier; p. 429–440.
   Google Scholar
• OCED. 2018. Working document on the risk assessment of secondary metabolites of microbial biocontrol agents (OECD Environment, Health and Safety Publications, Series on Pesticides, No. 98). Paris: OCED.
   Google Scholar
• Ottone C, Romero O, Urrutia P, Bernal C, Illanes A, Wilson L. 2021. Enzyme biocatalysis and sustainability. Nanostructured catalysts for environmental applications. Berlin, Germany: Springer; p. 383–413.
   Google Scholar
• Qasim F, Diercks‐Horn S, Gerlach D, Schneider A, Fernandez‐Lahore HM. 2022. Production of a novel milk‐clotting enzyme from solid‐substrate Mucor spp. culture. J Food Sci. 87(10):4348–4362. doi: 10.1111/1750-3841.16307.
   PubMed Web of Science ®Google Scholar
• Rähse W. 2014. Production of tailor‐made enzymes for detergents. Chem Bio Eng Rev. 1(1):27–39. doi: 10.1002/cben.201300001.
   Google Scholar
• Ratledge C, Kristiansen B. 2006. Basic biotechnology. New York (NY): Cambridge University Press; p. 219.
   Google Scholar
• Rieck HP. 2017. Builders: the backbone of powdered detergents. Powdered detergents. Abingdon: Routledge; p. 43–108.
   Google Scholar
• Saha P, Khan MF, Patra S. 2018. Truncated α-amylase: an improved candidate for textile processing. Prep Biochem Biotechnol. 48(7):635–645. doi: 10.1080/10826068.2018.1479863.
   PubMed Web of Science ®Google Scholar
• Sarrouh B, Santos TM, Miyoshi A, Dias R, Azevedo V. 2012. Up-to-date insight on industrial enzymes applications and global market. J Bioprocess Biotech. s1(01):002. doi: 10.4172/2155-9821.S4-002.
   Google Scholar
• Sayre TC, Lee TM, King NP, Yeates TO. 2011. Protein stabilization in a highly knotted protein polymer. Protein Eng Des Sel. 24(8):627–630. doi: 10.1093/protein/gzr024.
   PubMed Web of Science ®Google Scholar
• Shakilanishi S, Shanthi C. 2017. Specificity studies on proteases for dehairing in leather processing using decorin as model conjugated protein. Int J Biol Macromol. 103:1069–1076. doi: 10.1016/j.ijbiomac.2017.05.134.
   PubMed Web of Science ®Google Scholar
• Shire SJ, Shahrokh Z, Liu JUN. 2004. Challenges in the development of high protein concentration formulations. J Pharm Sci. 93(6):1390–1402. doi: 10.1002/jps.20079.
   PubMed Web of Science ®Google Scholar
• Singh A, Negi MS, Dubey A, Kumar V, Verma AK. 2018. Methods of enzyme immobilization and its applications in food industry. Enzymes in food technology. Singapore: Springer; p. 103–124.
   Google Scholar
• Singh R, Kim SW, Kumari A, Mehta PK. 2022. An overview of microbial α-amylase and recent biotechnological developments. CBIOT. 11(1):11–26. doi: 10.2174/2211550111666220328141044.
   Google Scholar
• Sundararajan S, Kannan CN, Chittibabu S. 2011. Alkaline protease from Bacillus cereus VITSN04: potential application as a dehairing agent. J Biosci Bioeng. 111(2):128–133. doi: 10.1016/j.jbiosc.2010.09.009.
   PubMed Web of Science ®Google Scholar
• Suzuki F, Ito N, Yuuki T, Yamagata H, Udaka S. 1989. Improving thermostability of raw-starch digesting amylase from a Cytophaga sp. by site-directed mutagenesis. J Biol Chem. 264(32):18933–18938. doi: 10.1016/S0021-9258(19)47247-5.
   PubMedGoogle Scholar
• Verma ML, Kumar S, Das A, Randhawa JS, Chamundeeswari M. 2020. Chitin and chitosan-based support materials for enzyme immobilization and biotechnological applications. Environ Chem Lett. 18(2):315–323. doi: 10.1007/s10311-019-00942-5.
   Web of Science ®Google Scholar
• Weijers SR, Van’t Riet K. 1992. Enzyme stability in downstream processing part 1: enzyme inactivation, stability and stabilization. Biotechnol Adv. 10(2):237–249. doi: 10.1016/0734-9750(92)90004-s.
   PubMed Web of Science ®Google Scholar
• Wintrode PL, Miyazaki K, Arnold FH. 2000. Cold adaptation of a mesophilic subtilisin like protease by laboratory evolution. J Biol Chem. 275(41):31635–31640. doi: 10.1074/jbc.M004503200.
   PubMed Web of Science ®Google Scholar
• Wu S, Snajdrova R, Moore JC, Baldenius K, Bornscheuer UT. 2021. Biocatalysis: enzymatic synthesis for industrial applications. Angew Chem Int Ed Engl. 60(1):88–119. doi: 10.1002/anie.202006648.
   PubMed Web of Science ®Google Scholar
• Yamaguchi S, Yamamoto E, Mannen T, Nagamune T, Nagamune T. 2013. Protein refolding using chemical refolding additives. Biotechnol J. 8(1):17–31. doi: 10.1002/biot.201200025.
   PubMed Web of Science ®Google Scholar
• Zbacnik TJ, Holcomb RE, Katayama DS, Murphy BM, Payne RW, Coccaro RC, Evans GJ, Matsuura JE, Henry CS, Manning MC. 2017. Role of buffers in protein formulations. J Pharm Sci. 106(3):713–733. doi: 10.1016/j.xphs.2016.11.014.
   PubMed Web of Science ®Google Scholar
• Zhang Y, He S, Simpson BK. 2018. Enzymes in food bioprocessing—novel food enzymes, applications, and related techniques. Curr Opin Food Sci. 19:30–35. doi: 10.1016/j.cofs.2017.12.007.
   Web of Science ®Google Scholar
• Zhao H. 2005. Effect of ions and other compatible solutes on enzyme activity, and its implication for biocatalysis using ionic liquids. J Mol Catal B Enzym. 37(1–6):16–25. doi: 10.1016/j.molcatb.2005.08.007.
   Google Scholar
• Zhou Z, Wang X. 2021. Rational design and structure-based engineering of alkaline pectate lyase from Paenibacillus sp. 0602 to improve thermostability. BMC Biotechnol. 21(1):32. doi: 10.1186/s12896-021-00693-8.
   PubMed Web of Science ®Google Scholar