Abstract
Proteases and lipases are significant groups of enzymes for commercialization at the global level. Earlier, the industries depended on mesophilic proteases and lipases, which remain nonfunctional under extreme conditions. The discovery of extremophilic microorganisms, especially those belonging to haloarchaea, paved a new reserve of industrially competent extremozymes. Haloarchaea or halophilic archaea are polyextremophiles of domain Archaea that grow at high salinity, elevated temperature, pH range (pH 6–12), and low aw. Interestingly, haloarchaeal proteolytic and lipolytic enzymes also perform their catalytic function in the presence of 4–5 M NaCl in vivo and in vitro. Also, they are of great interest to study due to their capacity to function and are active at elevated temperatures, tolerance to pH extremes, and in non-aqueous media. In recent years, advances have been achieved in various aspects of genomic/molecular expression methods involving homologous and heterologous processes for the overproduction of these extremozymes and their characterization from haloarchaea. A few protease and lipase extremozymes have been successfully expressed in prokaryotic systems, especially E.coli, and enzyme modification techniques have improved the catalytic properties of the recombinant enzymes. Further, in-silico methods are currently applied to elucidate the structural and functional features of salt-stable protease and lipase in haloarchaea. In this review, the production and purification methods, catalytic and biochemical properties and biotechnological applications of haloextremozymes proteases and lipases are summarized along with recent advancements in overproduction and characterization of these enzymes, concluding with the directions for further in-depth research on proteases and lipases from haloarchaea.
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References
Akmoussi-Toumi S, Khemili-Talbi S, Ferioune I, Kebbouche-Gana S (2018) Purification and characterization of an organic solvent-tolerant and detergent-stable lipase from Haloferax mediterranei CNCMM 50101. Int J Biol Macromol 116:817–830. https://doi.org/10.1016/j.ijbiomac.2018.05.087
Akolkar AV, Desai AJ (2010) Catalytic and thermodynamic characterization of protease from Halobacterium sp. SP1(1). Res Microbiol 161:355–362. https://doi.org/10.1016/j.resmic.2010.04.005
Akolkar AV, Deshpande GM, Raval KN, Durai D, Nerurkar AS, Desai AJ (2008) Organic solvent tolerance of Halobacterium sp. SP1 (1) and its extracellular protease. J Basic Microbiol 48(5):421–425
Akolkar A, Bharambe N, Trivedi S, Desai A (2009) Statistical optimization of medium components for extracellular protease production by an extreme haloarchaeon, Halobacterium sp. SP1(1). Lett Appl Microbiol 48:77–83. https://doi.org/10.1111/j.1472-765X.2008.02492.x
Akolkar AV, Durai D, Desai AJ (2010) Halobacterium sp. SP1 (1) as a starter culture for accelerating fish sauce fermentation. J Appl Microbiol 109(1):44–53
Allers T (2010) Overexpression and purification of halophilic proteins in Haloferax volcanii. Bioengineered Bugs 4:290–292. https://doi.org/10.4161/bbug.1.4.11794
Amoozegar MA, Siroosi M, Atashgahi S et al (2017) Systematics of haloarchaea and biotechnological potential of their hydrolytic enzymes. Microbiol (United Kingdom) 163:623–645. https://doi.org/10.1099/mic.0.000463
Aouad M, Taib N, Oudart A, Lecocq M, Gouy M, Brochier-Armanet C (2018) Extreme halophilic archaea derive from two distinct methanogen class II lineages. Mol Phylogenet Evol 127:46–54
Arpigny JL, Jaeger KE (1999) Bacterial lipolytic enzymes: classification and properties. Biochem J 343(1):177–183
Bhatnagar T, Boutaiba S, Hacene H et al (2005) Lipolytic activity from Halobacteria: screening and hydrolase production. FEMS Microbiol Lett 248:133–140. https://doi.org/10.1016/j.femsle.2005.05.044
Botos I, Melnikov EE, Cherry S, Tropea JE, Khalatova AG, Rasulova F, Gustchina A (2004) The catalytic domain of Escherichia coli Lon protease has a unique fold and a ser-lys dyad in the active site. J Biol Chem 279(9):8140–8148
Boutaiba S, Bhatnagar T, Hacene H et al (2006) Preliminary characterisation of a lipolytic activity from an extremely halophilic archaeon, Natronococcus sp. J Mol Catal B: Enzymatic 41:21–26. https://doi.org/10.1016/j.molcatb.2006.03.010
Brandstetter H, Kim JS, Groll M, Huber R (2001) Crystal structure of the tricorn protease reveals a protein disassembly line. Nature 414(6862):466–470
Brenner S (1988) The molecular evolution of genes and proteins: a tale of two serines. Nature 334:528–530
Camacho RM, Mateos JC, González-Reynoso O et al (2009) Production and characterization of esterase and lipase from Haloarcula marismortui. J Ind Microbiol Biotechnol 36:901–909. https://doi.org/10.1007/s10295-009-0568-1
Camacho RM, Mateos-Díaz JC, Diaz-Montaño DM et al (2010) Carboxyl ester hydrolases production and growth of a halophilic archaeon, Halobacterium sp. NRC-1. Extremophiles 14:99–106. https://doi.org/10.1007/s00792-009-0291-x
Capiralla H, Hiroi T, Hirokawa T, Maeda S (2002) Purification and characterization of a hydrophobic amino acid-specific endopeptidase from Halobacterium halobium S9 with potential application in debittering of protein hydrolysates. Process Biochem 38:571–579. https://doi.org/10.1016/S0032-9592(02)00180-2
Castro RE, De, Ruiz DM, Giménez MI et al (2008) Gene cloning and heterologous synthesis of a haloalkaliphilic extracellular protease of Natrialba magadi (Nep). Extremophiles 12:677–687. https://doi.org/10.1007/s00792-008-0174-6.Gene
Chen CKM, Lee GC, Ko TP, Guo RT, Huang LM, Liu HJ, Wang AHJ (2009) Structure of the alkalohyperthermophilic Archaeoglobus fulgidus lipase contains a unique C-terminal domain essential for long-chain substrate binding. J Mol Biol 390(4):672–685
Chuprom J, Bovornreungroj P, Ahmad M et al (2016) Approach toward enhancement of halophilic protease production by Halobacterium sp. strain LBU50301 using statistical design response surface methodology. Biotechnol Rep 10:17–28. https://doi.org/10.1016/j.btre.2016.02.004
Cui HL, Dyall-Smith ML (2021) Cultivation of halophilic archaea (class Halobacteria) from thalassohaline and athalassohaline environments. Mar Life Sci Technol 3:243–251
da Silva RR (2017) Bacterial and fungal proteolytic enzymes: production, catalysis and potential applications. Appl Biochem Biotechnol 183. https://doi.org/10.1007/s12010-017-2427-2
Dammak DF, Smaoui SM, Ghanmi F et al (2016) Characterization of halo-alkaline and thermostable protease from Halorubrum ezzemoulense strain ETR14 isolated from Sfax solar saltern in Tunisia. J Basic Microbiol 56:337–346. https://doi.org/10.1002/jobm.201500475
Das D (2019) Bioprospecting of Halophilic Archaea from Indian Solar Salterns. PhD Dissertation
De Castro RE, Maupin-Furlow JA, Giménez MI et al (2006) Haloarchaeal proteases and proteolytic systems. FEMS Microbiol Rev 30:17–35
Delfosse V, Girard E, Birck C, Delmarcelle M, Delarue M, Poch O, Mayer C (2009) Structure of the archaeal pab87 peptidase reveals a novel self-compartmentalizing protease family. PLoS ONE 4(3):e4712
Delgado-García M, Rodríguez JA, Mateos-Díaz JC, Aguilar CN, Rodríguez-Herrera R (2018) and RMC-R Halophilic Archaeal Lipases and Esterases: Activity, Stability, and Food Applications. In: M. Kuddus (ed.), Enzymes in Food Technology,. pp 243–262
Dodson G, Wlodawer A (1998) Catalytic triads and their relatives. Trends Biochem Sci 23(9):347–352
Elbanna K, Ibrahim IM, Revol-Junelles AM (2015) Purification and characterization of halo-alkali-thermophilic protease from Halobacterium sp. strain HP25 isolated from raw salt, Lake Qarun, Fayoum, Egypt. Extremophiles 19:763–774. https://doi.org/10.1007/s00792-015-0752-3
Franzetti B, Schoehn G, Hernandez JF, Jaquinod M, Ruigrok RWH, Zaccai G (2002) Tetrahedral aminopeptidase: a novel large protease complex from archaea. EMBO J 21(9):2132–2138
Gao R, Shi T, Liu X et al (2017) Purification and characterisation of a salt-stable protease from the halophilic archaeon Halogranum rubrum. J Sci Food Agric 97:1412–1419. https://doi.org/10.1002/jsfa.7879
Gaonkar SK, Furtado IJ (2018) Isolation and culturing of protease- and lipase-producing Halococcus agarilyticus GUGFAWS-3 from marine Haliclona sp. inhabiting the rocky intertidal region of Anjuna in Goa, India. Ann Microbiol 68:851–861. https://doi.org/10.1007/s13213-018-1391-6
Gaonkar SK, Furtado IJ (2020) Characterization of Extracellular protease from the Haloarcheon Halococcus sp. Strain GUGFAWS-3 (MF425611). Curr Microbiol 77:1024–1034. https://doi.org/10.1007/s00284-020-01896-6
Gaonkar SK, Furtado IJ (2021) Valorization of low-cost agro-wastes residues for the maximum production of protease and lipase haloextremozymes by Haloferax lucentensis GUBF-2 MG076078. Process Biochem 101:72–88. https://doi.org/10.1016/j.procbio.2020.10.019
Gaonkar SK, Furtado IJ (2022) Simultaneous purification and characterization of detergent-stable, solvent-tolerant haloextremozymes protease and lipase from Haloferax sp. strain GUBF 2. Arch Microbiol 1–16. https://doi.org/10.1007/s00203-022-03286-x
Giménez MI, Studdert CA, Sánchez JJ, De Castro RE (2000) Extracellular protease of Natrialba magadii: purification and biochemical characterization. Extremophiles 4:181–188. https://doi.org/10.1007/s007920070033
Gupta M, Aggarwal S, Navani NK, Choudhury B (2015) Isolation and characterization of a protease-producing novel haloalkaliphilic bacterium Halobiforma sp. strain BNMIITR from Sambhar lake in Rajasthan, India. Ann Microbiol 65:677–686. https://doi.org/10.1007/s13213-014-0906-z
Gupta RS, Naushad S, Fabros R, Adeolu M (2016) A phylogenomic reappraisal of family-level divisions within the class Halobacteria: proposal to divide the order Halobacteriales into the families Halobacteriaceae, Haloarculaceae fam. nov., and Halococcaceae fam. nov., and the order Haloferacales into the families, Haloferacaceae and Halorubraceae fam nov. Antonie Van Leeuwenhoek 109:565–587
Han D, Hou J, Cui HL (2023) An extracellular protease containing a novel C-terminal extension produced by a marine-originated haloarchaeon. Front Mar Sci 10:1–13. https://doi.org/10.3389/fmars.2023.1166287
Hanlon GW, Norman A (1981) Bacitracin and protease production in relation to Sporulation during Exponential growth of Bacillus licheniformis poorly utilized Carbon and Nitrogen sources. J Bacteriol 147:427–431
Haque RU, Paradisi F, Allers T (2019) Haloferax volcanii as immobilised whole cell biocatalyst: new applications for halophilic systems. Appl Microbiol Biotechnol 3807–3817. https://doi.org/10.1007/s00253-019-09725-y
Haque RU, Paradisi F, Allers T (2020) Haloferax volcanii for biotechnology applications: challenges, current state and perspectives. Appl Microbiol Biotechnol 104:1371–1382. https://doi.org/10.1007/s00253-019-10314-2
Hasan F, Shah AA, Hameed A (2006) Industrial applications of microbial lipases. Enzym Microb Technol 39(2):235–251
Hausmann S, Jaeger KE (2010) Lipolytic enzymes from bacteria. In Handbook of hydrocarbon and lipid microbiology 1099–1126
Hou J, Han J, Cai L et al (2014) Characterization of genes for chitin catabolism in Haloferax mediterranei. Appl Microbiol Biotechnol 98:1185–1194. https://doi.org/10.1007/s00253-013-4969-8
Hou J, Han D, Zhou Y et al (2020) Identification and characterization of the gene encoding an extracellular protease from haloarchaeon Halococcus salifodinae. Microbiol Res 236:126468. https://doi.org/10.1016/j.micres.2020.126468
Hou J, Yin X, Li Y et al (2021) Biochemical characterization of a low salt-adapted extracellular protease from the extremely halophilic archaeon Halococcus salifodinae. Int J Biol Macromol 176:253–259. https://doi.org/10.1016/j.ijbiomac.2021.02.081
Hou J, Li SY, Zhao YJ et al (2022) A novel halolysin without C-terminal extension from an extremely halophilic archaeon. Appl Microbiol Biotechnol 106(8):3009–3019
Izotova LS, Strongin AY, Chekulaeva LN et al (1983) Purification and properties of serine protease from Halobacterium halobium. J Bacteriol 155:826–830. 0021-9193/83/080826-05$02.00/0
Kamekura M, Seno Y (1990) A halophilic extracellular protease from a halophilic archaebacterium strain 172 P1. Biochem Cell Biol 68:352–359. https://doi.org/10.1139/o90-048
Kamekura M, Seno Y (1993) Partial sequence of the gene for a serine-protease from a Halophilic Archaeum Haloferax mediterranei R4, and nucleotide-sequences of 16S ribosomal-rna-encoding genes from several Halophilic Archaea. Experientia 49:503–513
Kamekura M, Seno Y, Holmes Ml, Dyall-Smith ML (1992) Molecular cloning and sequencing of the gene for a Halophilic Alkaline Serine protease (Halolysin) from an unidentified Halophilic Archaea strain (172P1) and expression of the gene in Haloferax volcanii. J Bacteriol 174. https://doi.org/10.1128/jb.174.3.736-742.1992
Kamekura M, Seno Y, Dyall-Smith M (1996) Halolysin R4, a serine proteinase from the halophilic archaeon Haloferax mediterranei; gene cloning, expression and structural studies. Biochim Biophys Acta 1294:159–167
Kennedy SP, Ng WV, Salzberg SL et al (2001) Understanding the adaptation of Halobacterium Species NRC-1 to its Extreme Environment through computational analysis of its genome sequence. Genome Res 11:1641–1650. https://doi.org/10.1101/gr.190201
Khan FI, Lan D, Durrani R, Huan W, Zhao Z, Wang Y (2017) The lid domain in lipases: structural and functional determinant of enzymatic properties. Front Bioeng Biotechnol 5:16
Kim J, Dordick JS (1997) Unusual salt and solvent dependence of a protease from an extreme halophile. Biotechnol Bioeng 55:471–479. https://doi.org/10.1002/(SICI)1097-0290(19970805)55:3<471::AID-BIT2>3.0.CO;2-9
Kovacic F, Babic N, Krauss U, Jaeger KE (2019) Classification of lipolytic enzymes from bacteria. Aerobic Utilization of Hydrocarbons Oils and Lipids 24:255–289
Li X, Yu HY (2014) Characterization of an organic solvent-tolerant lipase from Haloarcula sp. G41 and its application for biodiesel production. Folia Microbiol 59:455–463. https://doi.org/10.1007/s12223-014-0320-8
Lotti M, Grandori R, Fusetti F et al (1993) Cloning and analysis of Candida cylindracea lipase sequences. Gene 124:45–55. https://doi.org/10.1016/0378-1119(93)90760-Z
Mani K, Taib N, Hugoni M, Bronner G, Bragança JM, Debroas D (2020) Transient dynamics of archaea and bacteria in sediments and brine across a salinity gradient in a solar saltern of Goa, India. Front Microbiol 11:1891
Manikandan M, Pašić L, Kannan V (2009) Purification and biological characterization of a halophilic thermostable protease from Haloferax lucentensis VKMM 007. World J Microbiol Biotechnol 25:2247–2256. https://doi.org/10.1007/s11274-009-0132-1
Manjula R (2014) Protease production by haloarchaea Natrinema sp. BTSH10 isolated from salt pan of South India
Martin del Campo M, Camacho RM, Mateos-Díaz JC et al (2015) Solid-state fermentation as a potential technique for esterase/lipase production by halophilic archaea. Extremophiles 19:1121–1132. https://doi.org/10.1007/s00792-015-0784-8
Martínez-Espinosa RM (2020) Heterologous and homologous expression of proteins from haloarchaea: denitrification as case of study. Int J Mol Sci 21. https://doi.org/10.3390/ijms21010082
Matsumoto T, Ito M, Fukuda H, Kondo A (2004) Enantioselective transesterification using lipase-displaying yeast whole-cell biocatalyst. Appl Microbiol Biotechnol 64:481–485. https://doi.org/10.1007/s00253-003-1486-1
Meghwanshi GK, Verma S, Srivastava V, Kumar R (2022) Archaeal lipolytic enzymes: current developments and further prospects. Biotechnol Adv 61:108054. https://doi.org/10.1016/j.biotechadv.2022.108054
Mokashe N, Chaudhari B, Patil U (2018) Operative utility of salt-stable proteases of halophilic and halotolerant bacteria in the biotechnology sector. Int J Biol Macromol 117:493–522
Müller-Santos M, de Souza EM, Pedrosa F, de O et al (2009) First evidence for the salt-dependent folding and activity of an esterase from the halophilic archaea Haloarcula marismortui. Biochim et Biophys Acta - Mol Cell Biology Lipids 1791:719–729. https://doi.org/10.1016/j.bbalip.2009.03.006
Nolasco H, Kushner D, Ochoa J-L (2002) Purification and Properties of an Extracellular Halophilic serine-protease from Haloferax mediterranei. J Mex Chem Soc 46:202–211
Norberg P, Hofsten B (1969) Proteolytic enzymes from extremely halophilic Bacteria. J Gen Microbiol 55:251–256
Oren A (2013) Life at high salt concentrations, intracellular KCl concentrations, and acidic proteomes. Front Microbiol 4:315
Oren A (2014) Halophilic archaea on Earth and in space: growth and survival under extreme conditions. Philosophical Trans Royal Soc A: Math Phys Eng Sci 372(2030):20140194
Ozcan B, Ozyilmaz G, Cokmus C, Caliskan M (2009) Characterization of extracellular esterase and lipase activities from five halophilic archaeal strains. J Ind Microbiol Biotechnol 36:105–110. https://doi.org/10.1007/s10295-008-0477-8
Ozcan B, Ozyilmaz G, Cihan A et al (2012) Phylogenetic analysis and characterization of lipolytic activity of halophilic archaeal isolates. Microbiology 81:186–194. https://doi.org/10.1134/S0026261712020105
Rao L, Zhao X, Pan F et al (2009) Solution behavior and activity of a halophilic esterase under high salt concentration. PLoS ONE 4. https://doi.org/10.1371/journal.pone.0006980
Rawlings ND, Barrett AJ (1994) Classification of peptidases. Methods Enzymol 244:1–15
Rawlings ND, Bateman A (2019) Origins of peptidases. Biochimie 166:4–18
Rawlings ND, Tolle DP, Barrett AJ (2004) MEROPS: the peptidase database. Nucleic Acids Res 32:D160–D164
Rawlings ND, Barrett AJ, Bateman A (2011) Asparagine peptide lyases: a seventh catalytic type of proteolytic enzymes. J Biol Chem 286(44):38321–38328
Ruiz DM, De Castro RE (2007) Effect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii. J Ind Microbiol Biotechnol 34:111–115. https://doi.org/10.1007/s10295-006-0174-4
Ruiz DM, Iannuci NB, Cascone O, Castro RE, De (2010) Peptide synthesis catalysed by a haloalkaliphilic serine protease from the archaeon Natrialba magadii (nep). Appl Microbiol 691–696. https://doi.org/10.1111/j.1472-765X.2010.02955.x
Russo S, Baumann U (2004) Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase. J Biol Chem 279(49):51275–51281
Ryu K, Kim J, Dordick JS (1994) Catalytic properties and potential of an extracellular protease from an extreme halophile. Enzyme Microb Technol 16:266–275
Salihu A, Alam MZ (2015) Solvent tolerant lipases: a review. Process Biochem 50:86–96. https://doi.org/10.1016/j.procbio.2014.10.019
Schmitt W, RU and GW (1990) Efficient high-performance liquid chromatographic system for the purification of a halobacterial serine protease. J Chromatogr 521:211–220
Schoehn G, Vellieux FM, Dura MA, Receveur-Bréchot V, Fabry CM, Ruigrok RW, Franzetti B (2006) An archaeal peptidase assembles into two different quaternary structures. J Biol Chem 281(47):36327–36337
Selim S, Hagagy N, Aziz MA, El-Meleigy ES, Pessione E (2014) Thermostable alkaline halophilic-protease production by Natronolimnobius innermongolicus WN18. Nat Prod Res 28(18):1476–1479
Shi W, Tang XF, Huang Y et al (2006) An extracellular halophilic protease SptA from a halophilic archaeon Natrinema sp. J7: gene cloning, expression and characterization. Extremophiles 10:599–606. https://doi.org/10.1007/s00792-006-0003-8
Singh A, Singh AK (2017) Haloarchaea: worth exploring for their biotechnological potential. Biotechnol Lett 39:1793–1800. https://doi.org/10.1007/s10529-017-2434-y
Singh A, Singh AK (2018) Isolation, characterization and exploring biotechnological potential of halophilic archaea from salterns of western India. 3 Biotech 8:45. https://doi.org/10.1007/s13205-017-1072-3
Sivakumar N, Li N, Tang JW et al (2006) Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition. FEBS Lett 580:2646–2652. https://doi.org/10.1016/j.febslet.2006.04.017
Stan-Lotter H, Doppler E, Jarosch M et al (1999) Isolation of a chymotrypsinogen B-like enzyme from the archaeon Natronomonas pharaonis and other halobacteria. Extremophiles 3:153–161. https://doi.org/10.1007/s007920050111
Stepanov VM, Rudenskaya GN, Revina LP et al (1992) A serine proteinase of an archaebacterium, Halobacterium mediterranei. A homologue of eubacterial subtilisins. Biochem J 285:281–286. https://doi.org/10.1042/bj2850281
Studdert Ca, De Castro RE, Seitz KH, Sánchez JJ (1997) Detection and preliminary characterization of extracellular proteolytic activities of the haloalkaliphilic archaeon Natronococcus occultus. Arch Microbiol 168:532–535. https://doi.org/10.1007/s002030050532
Studdert CA, Seitz MKH, Gil MIP et al (2001) Purification and biochemical characterization of the haloalkaliphilic archaeon Natronococcus occultus extracellular serine protease. J Basic Microbiol 41:375–383. https://doi.org/10.1002/1521-4028(200112)41:6<375::AID-JOBM375>3.0.CO;2-0
Sysoev M, Grötzinger SW, Renn D, Eppinger J, Rueping M, Karan R (2021) Bioprospecting of novel extremozymes from prokaryotes- the advent of culture-independent methods. Front Microbiol 12:630013
Verma S, Meghwanshi GK, Kumar R (2018) Structural homogeneity in microbial lipases. Environments 8:738–748
Verma S, Kumar R, Meghwanshi GK (2019) Identification of new members of alkaliphilic lipases in archaea and metagenome database using reconstruction of ancestral sequences. 3 Biotech 9:1–8
Verma S, Kumar R, Kumar P, Sharma D, Gahlot H, Sharma PK, Meghwanshi GK (2020) Cloning, characterization, and structural modeling of an extremophilic bacterial lipase isolated from saline habitats of the Thar desert. Appl Biochem Biotechnol 192:557–572
Vidyasagar M, Prakash S, Litchfield C, Sreeramulu K (2006) Purification and characterization of a thermostable, haloalkaliphilic extracellular serine protease from the extreme halophilic archaeon Halogeometricum borinquense strain TSS101. Archaea (Vancouver BC) 2:51–57. https://doi.org/10.1155/2006/430763
VijayAnand S, Hemapriya J, Selvin J (2010) Production and optimization of haloalkaliphilic protease by an extremophile-Halobacterium sp. Js1, isolated from thalassohaline environment. Global J Biotechnol 5:44–49
Vijayaraghavan P, Jebamalar TRJ, Vincent SGP (2012) Biosynthesis optimization and purification of a solvent stable alkaline serine protease from Halobacterium sp. Ann Microbiol 62:403–410. https://doi.org/10.1007/s13213-011-0276-8
Zhang Y, Wang M, Du X et al (2014) Chitin accelerates activation of a novel haloarchaeal serine protease that deproteinizes chitin-containing biomass. Appl Environ Microbiol 80:5698–5708. https://doi.org/10.1128/AEM.01196-14
Zhang S, Chen F, Ke J et al (2023) Hly176B, a low-salt tolerant halolysin from the haloarchaeon Haloarchaeobius sp. FL176. World J Microbiol Biotechnol 39:189. https://doi.org/10.1007/s11274-023-03632-1
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Author SG acknowledges Research studentship, Goa University (Grant No. GU/ Acad-PG/Ph.D./Res.Stud./2017-18/211).
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Gaonkar, S.K., Alvares, J.J. & Furtado, I.J. Recent advances in the production, properties and applications of haloextremozymes protease and lipase from haloarchaea. World J Microbiol Biotechnol 39, 322 (2023). https://doi.org/10.1007/s11274-023-03779-x
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DOI: https://doi.org/10.1007/s11274-023-03779-x