Abstract
Advanced developments in the field of enzyme technology have increased the use of enzymes in industrial applications, especially in detergents. Enzymes as detergent additives have been extensively studied and the demand is considerably increasing due to its distinct properties and potential applications. Enzymes from microorganisms colonized at various geographical locations ranging from extreme hot to cold are explored for compatibility studies as detergent additives. Especially psychrophiles growing at cold conditions have cold-active enzymes with high catalytic activity and their stability under extreme conditions makes it as an appropriate eco-friendly and cost-effective additive in detergents. Adequate number of reports are available on cold-active enzymes such as proteases, lipases, amylases, and cellulases with high efficiency and exceptional features. These enzymes with increased thermostability and alkaline stability have become the premier choice as detergent additives. Modern approaches in genomics and proteomics paved the way to understand the compatibility of cold-active enzymes as detergent additives in broader dimensions. The molecular techniques such as gene coding, amino acid sequencing, and protein engineering studies helped to solve the mysteries related to alkaline stability of these enzymes and their chemical compatibility with oxidizing agents. The present review provides an overview of cold-active enzymes used as detergent additives and molecular approaches that resulted in development of these enzymes as commercial hit in detergent industries. The scope and challenges in using cold-active enzymes as eco-friendly and sustainable detergent additive are also discussed.
Similar content being viewed by others
References
Arabaci N, Arikan B (2018) Isolation and characterization of a cold-active, alkaline, detergent stable α-amylase from a novel bacterium Bacillus subtilis N8. Prep Biochem Biotechnol 48(5):419–426. https://doi.org/10.1080/10826068.2018.1452256
Baghel VS, Tripathi RD, Ramteke PW, Gopal K, Dwivedi S, Rai UN, Singh SN (2005) Psychrotrophic proteolytic bacteria from cold environment of Gangotri glacier, Western Himalaya, India. Enzym Microb Technol 36(5–6):654–659. https://doi.org/10.1016/j.enzmictec.2004.09.005
Bakermans C, Skidmore ML (2011) Microbial metabolism in ice and brine at −5 degrees C. Environ Microbiol 13:2269–2278. https://doi.org/10.1111/j.1462-2920.2011.02485.x
Boetius A, Anesio AM, Deming JW, Mikucki JA, Rapp JZ (2015) Microbial ecology of the cryosphere: sea ice and glacial habitats. Nat Rev Microbiol 13:677. https://doi.org/10.1038/nrmicro3522
Cary SC, McDonald IR, Barrett JE, Cowan DA (2010) On the rocks: the microbiology of Antarctic dry valley soils. Nat Rev Microbiol 8(2):129–138. https://doi.org/10.1038/nrmicro2281
Cavicchioli R, Charlton T, Ertan H, Mohd Omar S, Siddiqui KS, Williams TJ (2011) Biotechnological uses of enzymes from psychrophiles. Microb Biotechnol 4:449–460. https://doi.org/10.1111/j.1751-7915.2011.00258.x
Chauhan PS, Puri N, Sharma P, Gupta KN (2012) Mannanases: microbial sources, production, properties and potential biotechnological applications. Appl Microbiol Biotechnol 93:1817–1830. https://doi.org/10.1007/s00253-012-3887-5
Chintalapati S, Kiran MD, Shivaji S (2004) Role of membrane lipid fatty acids in cold adaptation. Cell Mol Biol (Noisy-le-grand) 50:631–642
Cowan-Ellsberry C, Belanger S, Dorn P, Dyer S, McAvoy D, Sanderson H, Versteeg D, Ferrer D, Stanton K (2014) Environmental safety of the use of major surfactant classes in North America. Crit Rev Environ Sci Technol 44:1893–1993. https://doi.org/10.1080/10739149.2013.803777
Csiszar E, Losonczi A, Szakacs G, Rusznak I, Bezur L, Reicher J (2001a) Enzymes and chelating agent in cotton pretreatment. J Biotechnol 89(2):271–279. https://doi.org/10.1016/s0168-1656(01)00315-7
Csiszar E, Urbanszki K, Szakacs G (2001b) Biotreatment of desized cotton fabrics by commercial cellulase and xylanase enzymes. J Mol Catal B Enzym 11(4–6):1065–1072. https://doi.org/10.1016/S1381-1177(00)00149-1
D’Amico S, Collins T, Marx JC, Feller G, Gerday C (2006) Psychrophilic microorganisms: challenges for life. EMBO Rep 7:385–389. https://doi.org/10.1038/sj.embor.7400662
Davail S, Feller G, Narinx E, Gerday C (1994) Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the Antarctic psychrophile Bacillus TA41. J Biol Chem 269:17448–17453
De Maayer P, Anderson D, Cary C, Cowan DA (2014) Some like it cold: understanding the survival strategies of psychrophiles. EMBO Rep 15:508–517. https://doi.org/10.1002/embr.201338170
Degani O, Gepstein S, Dosoretz CG (2002) Potential use of cutinase in enzymatic scouring of cotton fiber cuticle. Appl Biochem Biotechnol 103(1):277–290. https://doi.org/10.1385/ABAB:102-103:1-6:277
Feller G (2010) Protein stability and enzyme activity at extreme biological temperatures. J Phys Condens Matter 22:323101. https://doi.org/10.1088/0953-8984/22/32/323101
Friedmann EI (1982) Endolithic microorganisms in the Antarctic cold desert. Science 215(4536):1045–1053. https://doi.org/10.1126/science.215.4536.1045
Furhana J, Awasthib P, Sharmaa S (2019) Biochemical characterization and homology modelling of cold-active alkophilic protease from Northwestern Himalayas and its application in detergent industry. Biocatal Agric Biotechnol 17:726–735. https://doi.org/10.1016/j.bcab.2019.01.028
Gerday C (2013) Psychrophily and catalysis. Biology 2:719–741. https://doi.org/10.3390/biology2020719
Herbots I, Kottwitz B, Reilly PJ, Antrim RL, Burrows H, Lenting HBM, Viikari L, Suurnakki A, Niku-paavola M, Pere J, Buchert J (2000) Enzymes, non-food application. In: Ullmann’s encyclopedia of industrial chemistry. Wiley-VCH Verlag GmbH & Co. KGaA, New Jersey
Hmidet N, Ali N, Haddar A, Kanoun S, Alya S, Nasri M (2009) Alkaline proteases and thermostable α-amylase co-produced by Bacillus licheniformis NH1: characterization and potential application as detergent additive. Biochem Eng J 47:71–79. https://doi.org/10.1016/j.bej.2009.07.005
Horn SJ, Vaaje-Kolstad G, Westereng B, Eijsink VG (2012) Novel enzymes for the degradation of cellulose. Biotechnol Biofuels 5(1):45. https://doi.org/10.1186/1754-6834-5-45
Jakob F, Martinez R, Mandawe J, Hellmuth H, Siegert P, Maurer KH, Schwaneberg U (2013) Surface charge engineering of a Bacillus gibsonii subtilisin protease. Appl Microbiol Biotechnol 97:6793–6802. https://doi.org/10.1007/s00253-012-4560-8
Ji X, Chen G, Zhang Q, Lin L (2015) Purification and characterization of an extracellular cold-adapted alkaline lipase produced by psychrotrophic bacterium Yersinia enterocolitica strain KM1. J Basic Microbiol 55(6):718–728. https://doi.org/10.1002/jobm.201400730
Joseph B (2006) Isolation, purification and characterization of cold adapted extracellular lipases from psychrotrophic bacteria: feasibility as laundry detergent additive. Ph.D dissertation Allahabad Agricultural Institute-Deemed University, Allahabad
Joseph B, Ramteke PW (2013) Extracellular solvent stable cold active lipase from psychrotrophic Bacillus sphaericus MTCC 7526: partial purification and characterization. Ann Microbiol 63:363–370. https://doi.org/10.1007/s13213-012-0483-y
Joseph B, Ramteke PW, Thomas G (2008) Cold active microbial lipases: some hot issues and recent developments. Biotechnol Adv 26:457–470. https://doi.org/10.1016/j.biotechadv.2008.05.003
Joseph B, Shrivastava N, Ramteke PW (2012) Extracellular cold-active lipase of Microbacterium luteolum isolated from Gangotri glacier, Western Himalaya: isolation, partial purification and characterization. J Genet Eng Biotechnol 10:137–144. https://doi.org/10.1016/j.jgeb.2012.02.001
Joshi S, Satyanarayana T (2013) Biotechnology of cold-active proteases. Biology 2:755–783. https://doi.org/10.3390/biology2020755
Jurado E, Bravo V, Luzon G, Fernandez-Serrano M, Garcia-Roman M, Altmajer-Vaz D, Vicaria JM (2007) Hard-surface cleaning using lipases: enzyme–surfactant interactions and washing tests. J Surfactant Deterg 10:61–70. https://doi.org/10.1007/s11743-006-1009-z
Karan R, Capes MD, DasSarma S (2012) Function and biotechnology of extremophilic enzymes in low water activity. Aquatic Biosystems 8(1):4
Karmakar M, Ray RR (2011) Current trends in research and application of microbial cellulases. Res J Microbiol 6(1):41–53. https://doi.org/10.3923/jm.2011.41.53
Kasana RC, Gulati A (2011) Cellulases from psychrophilic microorganisms: a review. J Basic Microbiol 51:572–579. https://doi.org/10.1002/jobm.201000385
Kavitha M, Shanthi C (2017) Alkaline thermostable cold active lipase from halotolerant Pseudomonas sp. VITCLP4 as detergent additive. Indian J Biotechnol 6:446–455 http://nopr.niscair.res.in/handle/123456789/43324
Ke MM, Ramesh B, Hang YA, Liu ZD (2018) Engineering and characterization of a novel low temperature active and thermo stable esterase from marine. Enterobacter cloacae. Int J Biol Macromol 118:304–310. https://doi.org/10.1016/j.ijbiomac.2018.05.193
Kim S, Lee MH, Lee ES, Nam YD, Seo DH (2018) Characterization of mannanase from Bacillus sp., a novel Codium fragile cell wall-degrading bacterium. Food Sci Biotechnol 27:115–122. https://doi.org/10.1007/s10068-017-0210-3
Kuddus M, Ramteke PW (2009) Cold-active extracellular alkaline protease from an alkaliphilic Stenotrophomonas maltophilia: production of enzyme and its industrial applications. Can J Microbiol 55:1294–1301. https://doi.org/10.1139/w09-089
Kuddus M, Ramteke PW (2011) Production optimization of an extracellular cold-active alkaline protease from Stenotrophomonas maltophilia MTCC 7528 and its application in detergent industry. Afr J Microbiol Res 5(7):809–816. https://doi.org/10.5897/AJMR10.806
Kuddus M, Ramteke PW (2012) Recent developments in production and biotechnological applications of cold-active microbial proteases. Crit Rev Microbiol 38:380–388. https://doi.org/10.3109/1040841X.2012.678477
Kumari U, Singh R, Ray T, Rana S, Saha P, Malhotra K, Daniell H (2019) Validation of leaf enzymes in the detergent and textile industries: launching of a new platform technology. Plant Biotechnol J 17(6):1167–1182. https://doi.org/10.1111/pbi.13122
Langridge P, Morita RY (1966) Thermolability of malic dehydrogenase from the obligate psychrophile, Vibrio marinus. J Bacteriol 92:418–423
Li XL, Zhang WH, Wang YD, Dai YJ, Zhang HT, Wang Y, Wang HK, Lu FP (2014) A high-detergent-performance, cold-adapted lipase from Pseudomonas stutzeri PS59 suitable for detergent formulation. J Mol Catal B Enzym 102:16–24. https://doi.org/10.1016/j.molcatb.2014.01.006
Liu R, Jiang X, Mou H, Guan H, Hwang H, Li X (2009) A novel low-temperature resistant alkaline lipase from a soda lake fungus strain Fusarium solani N4-2 for detergent formulation. Biochem Eng J 46(3):265–270. https://doi.org/10.1016/j.bej.2009.05.016
Lu Z, Hu X, Shen P, Wang Q, Zhou Y, Zhang G, Ma Y (2018) A pH-stable, detergent and chelator resistant type I pullulanase from Bacillus pseudofirmus 703 with high catalytic efficiency. Int J Biol Macromol 109:1302–1310. https://doi.org/10.1016/j.ijbiomac.2017.11.139
Luetz S (2010) Reengineering enzymes. Science. 329:285–287. https://doi.org/10.1126/science.1192224
Mageswari A, Subramanian P, Chandrasekaran S, Karthikeyan S, Gothandam KM (2017) Systematic functional analysis and application of a cold-active serine protease from a novel Chryseobacterium sp. Food Chem 217:18–27. https://doi.org/10.1016/j.foodchem.2016.08.064
Maharana A, Ray P (2015) A novel cold-active lipase from psychrotolerant Pseudomonas sp. AKM-L5 showed organic solvent resistant and suitable for detergent formulation. J Mol Catal B Enzym 120:173–178. https://doi.org/10.1016/j.molcatb.2015.07.005
Mahmood Q, Shaheen S, Bilal M, Tariq M, Zeb BS, Ullah Z, Ali A (2019) Chemical pollutants from an industrial estate in Pakistan: a threat to environmental sustainability. Appl Water Sci 9:47–49. https://doi.org/10.1007/s13201-019-0920-1
Margesin R (2009) Cold active enzymes as new tools in biotechnology. Extremophiles-Vol II. In: Gerday C (ed) Extremophiles. Encyclopedia of life support systems Oxford
McDonald IJ, Chambers AK (1963) Some characteristics of proteinases of an obligately psychrophilic red-pigmented bacterium and of Serratia marcescens. Can J Microbiol 9:871–877. https://doi.org/10.1139/m63-114
Munoz PA, Marquez SL, Gonzalez-Nilo FD, Marquez-Miranda V, Blamey JM (2017) Structure and application of antifreeze proteins from Antarctic bacteria. Microb Cell Factories 16:1–13. https://doi.org/10.1186/s12934-017-0737-2
Mykytczuk NC, Foote SJ, Omelon CR, Southam G, Greer CW, Whyte LG (2013) Bacterial grow that −15 degrees C; molecular insights from the permafrost bacterium Planococcus halocryophilus Or. ISMEJ 7:1211–1226. https://doi.org/10.1038/ismej.2013.8
Niyonzima FN (2019) Detergent-compatible bacterial cellulases. J Basic Microbiol 59(2):134–147. https://doi.org/10.1002/jobm.201800436
Niyonzima FN, More SS (2014) Detergent-compatible bacterial amylases. Appl Biochem Biotechnol 174:1215–1232. https://doi.org/10.1007/s12010-014-1144-3
Park HJ, Han SJ, Yim JH, Kim D (2018) Characterization of an Antarctic alkaline protease, a cold-active enzyme for laundry detergents. Korean J Microbiol 54(1):60–68. https://doi.org/10.7845/kjm.2018.7080
Phadtare S (2004) Recent developments in bacterial cold-shock response. Curr Issues Mol Biol 6:125–136
Poulouse AJSB (1994) Selection and method of making enzymes for perhydrolysis system and for altering substrate specificity, specific activity and catalytic efficiency, patent US5352594 a
Qin Y, Huang Z, Liu Z (2014) A novel cold-active and salt-tolerant alpha-amylase from marine bacterium Zunongwangia profunda: molecular cloning, heterologous expression and biochemical characterization. Extremophiles 18:271–281. https://doi.org/10.1007/s00792-013-0614-9
Qoura F, Elleuche S, Brueck T, Antranikian G (2014) Purification and characterization of a cold-adapted pullulanase from a psychrophilic bacterial isolate. Extremophiles 18:1095–1102. https://doi.org/10.1007/s00792-014-0678-1
Rajaei S, Noghabi KA, Sadeghizadeh M, Zahiri HS (2015) Characterization of a pH and detergent-tolerant, cold-adapted type I pullulanase from Exiguobacterium sp. SH3. Extremophiles 19:1145–1155. https://doi.org/10.1007/s00792-015-0786-6
Ranjan K, Lone MA, Sahay S (2016) Detergent compatible cold-active alkaline amylases from Clavispora lusitaniae CB13. J Microbiol Biotechnol Food Sci 5:306–310. https://doi.org/10.15414/jmbfs.2016.5.4.306-310
Reed CJ, Lewis H, Trejo E, Winston V, Evilia C (2013) Protein adaptations in archaeal extremophiles. Archaea 373275. https://doi.org/10.1155/2013/373275
Roohi, Kuddus M, Saima (2013) Cold-active detergent-stable extracellular α-amylase from Bacillus cereus GA6: biochemical characteristics and its perspectives in laundry detergent formulation J Biochem Tech 4(4): 636–644
Russell AJ, Fersht AR (1987) Rational modification of enzyme catalysis by engineering surface-charge. Nature 328:496–500. https://doi.org/10.1038/328496a0
Saeki K, Ozaki K, Kobayashi T, Ito S (2007) Detergent alkaline proteases: enzymatic properties, genes, and crystal structures. J Biosci Bioeng 103:501–508. https://doi.org/10.1263/jbb.103.501
Sahay S, Chouhan D (2018) Study on the potential of cold-active lipases from psychrotrophic fungi for detergent formulation. J Genet Biotechnol 16(2):319–325. https://doi.org/10.1016/j.jgeb.2018.04.006
Sarmiento F, Peralta R, Blamey JM (2015) Cold and hot extremozymes: industrial relevance and current trends. Front Bioeng Biotechnol 3:148. https://doi.org/10.3389/fbioe.2015.00148
Showell MS (1999) Enzymes, detergents. In: Flickinger MC, Drew SW (eds) The encyclopedia of bioprocess technology, 2. Wiley, New York
Siddiqui KS, Cavicchioli R (2006) Cold-adapted enzymes. Annu Rev Biochem 75:403–433. https://doi.org/10.1146/annurev.biochem.75.103004.142723
Siddiqui KS, Williams TJ, Wilkins D, Yau S, Allen MA, Brown MV, Lauro FM, Cavicchioli R (2013) Psychrophiles. Annu Rev Earth Planet Sci 41:87–115. https://doi.org/10.1146/annurev-earth-040610-133514
Singh D, Thakur S, Thayil SM, Kesavan AK (2019) Characterization of a cold-active, detergent-stable metallopeptidase purified from Bacillus sp. S1DI 10 using Response Surface Methodology. PLoS One 14(5):e0216990. https://doi.org/10.1371/journal.pone.0216990
Singh R, Kumar M, Mittal A, Mehta PK (2016) Microbial enzymes: industrial progress in 21st century. 3. Biotech 6:174. https://doi.org/10.1007/s13205-016-0485-8
Souza TV, Araujo JN, da Silva VM, Liberato MV, Pimentel AC, Alvarez TM, Squina FM, Garcia W (2016) Chemical stability of a cold-active cellulase with high tolerance toward surfactants and chaotropic agent. Biotechnol Rep 9:1–8. https://doi.org/10.1016/j.btre.2015.11.001
Tavano OL (2013) Protein hydrolysis using proteases: an important tool for food biotechnology. J Mol Catal B Enzym 90:1–11. https://doi.org/10.1016/j.molcatb.2013.01.011
Tindbaek N, Svendsen A, Oestergaard PR, Draborg H (2004) Engineering a substrate specific cold-adapted subtilisin. PEDS 17:149–156. https://doi.org/10.1093/protein/gzh019
Tribelli PM, Lopez NI (2018) Reporting key features in cold-adapted bacteria. Life 8:E8. https://doi.org/10.3390/life8010008
Tynan-Connolly BM, Nielsen JE (2007) Redesigning protein pKa values. Protein Sci 16:239–249. https://doi.org/10.1110/ps.062538707
Vojcic L, Pitzler C, Korfer G, Jakob F, Martinez R, Maurer KH, Schwaneberg U (2015) Advances in protease engineering for laundry detergents. New Biotechnol 32(6):629–634. https://doi.org/10.1016/j.nbt.2014.12.010
Wackett LP (2019) Microbial industrial enzymes: an annotated selection of World Wide Web sites relevant to the topics in microbial biotechnology. Microb Biotechnol 12(5):1090–1091. https://doi.org/10.1111/1751-7915.13389
Wang Q, Fan X, Hua Z, Gao W, Chen J (2007) Degradation kinetics of pectins by an alkaline pectinase in bioscouring of cotton fabrics. Carbohydr Polym 67:572–575. https://doi.org/10.1016/j.carbpol.2006.06.031
Wang X, Kan G, Ren X, Yu G, Shi C, Xie Q, Wen H, Betenbaugh M (2018) Molecular cloning and characterization of a novel alpha-amylase from Antarctic Sea ice bacterium Pseudoalteromonas sp. M175 and its primary application in detergent. Biomed Res Int 2018:3258383. https://doi.org/10.1155/2018/3258383
Wintrode PL, Miyazaki K, Arnold FH (2000) Cold adaptation of a mesophilic subtilisin like protease by laboratory evolution. J Biol Chem 275:31635–31640. https://doi.org/10.1074/jbc.M004503200
Wong TS, Tee KL, Hauer B, Schwaneberg U (2004) Sequence saturation mutagenesis (SeSaM): a novel method for directed evolution. Nucleic Acids Res 32:e26. https://doi.org/10.1093/nar/gnh028
Zheng X, Chu X, Zhang W, Wu N, Fan Y (2011) A novel cold-adapted lipase from Acinetobacter sp. XMZ-26: gene cloning and characterization. Appl Microbiol Biotechnol 90:971–980. https://doi.org/10.1007/s00253-011-3154-1
Acknowledgments
The authors are thankful to the authorities of Shaqra University, Kingdom of Saudi Arabia, for all the necessary help to perform the related literature survey and research work.
Author information
Authors and Affiliations
Contributions
AAAG collected the data, formatted and wrote the manuscript. BJ formatted the figures, reviewed and corrected the manuscript. All authors read and approved the manuscript.
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that they have no conflict of interest.
Ethical approval
This article does not contain any studies with human participants or animals performed by any of the authors.
Additional information
Publisher’s note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Al-Ghanayem, A.A., Joseph, B. Current prospective in using cold-active enzymes as eco-friendly detergent additive. Appl Microbiol Biotechnol 104, 2871–2882 (2020). https://doi.org/10.1007/s00253-020-10429-x
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00253-020-10429-x