{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,17]],"date-time":"2026-03-17T20:35:43Z","timestamp":1773779743512,"version":"3.50.1"},"reference-count":77,"publisher":"Springer Science and Business Media LLC","issue":"2","license":[{"start":{"date-parts":[[2025,12,11]],"date-time":"2025-12-11T00:00:00Z","timestamp":1765411200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,12,11]],"date-time":"2025-12-11T00:00:00Z","timestamp":1765411200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/501100002964","name":"\u00c7ukurova \u00dcniversitesi","doi-asserted-by":"publisher","award":["FBA-2022-14816"],"award-info":[{"award-number":["FBA-2022-14816"]}],"id":[{"id":"10.13039\/501100002964","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002964","name":"\u00c7ukurova \u00dcniversitesi","doi-asserted-by":"publisher","award":["FDK-2017-9584"],"award-info":[{"award-number":["FDK-2017-9584"]}],"id":[{"id":"10.13039\/501100002964","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Appl Biochem Biotechnol"],"published-print":{"date-parts":[[2026,2]]},"DOI":"10.1007\/s12010-025-05481-0","type":"journal-article","created":{"date-parts":[[2025,12,11]],"date-time":"2025-12-11T09:35:34Z","timestamp":1765445734000},"page":"910-931","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Enzymatic Properties and Multifunctional Applications of a Novel Extracellular Cold-Active Alkaline Protease from Stenotrophomonas maltophilia Strain TK-4"],"prefix":"10.1007","volume":"198","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1723-209X","authenticated-orcid":false,"given":"Tuna","family":"Karaytug","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3829-6495","authenticated-orcid":false,"given":"Nihan","family":"Arabaci","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2868-7265","authenticated-orcid":false,"given":"Burhan","family":"Ar\u0131kan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2025,12,11]]},"reference":[{"issue":"10","key":"5481_CR1","doi-asserted-by":"publisher","first-page":"8532","DOI":"10.3390\/ijms24108532","volume":"24","author":"Z Yang","year":"2023","unstructured":"Yang, Z., Huang, Z., Wu, Q., Tang, X., & Huang, Z. (2023). Cold-adapted proteases: An efficient And energy-saving biocatalyst. International Journal of Molecular Sciences, 24(10), 8532. https:\/\/doi.org\/10.3390\/ijms24108532","journal-title":"International Journal of Molecular Sciences"},{"key":"5481_CR2","doi-asserted-by":"publisher","first-page":"148","DOI":"10.3389\/fbioe.2015.00148","volume":"3","author":"F Sarmiento","year":"2015","unstructured":"Sarmiento, F., Peralta, R., & Blamey, J. M. (2015). Cold and hot extremozymes: Industrial relevance and current trends. Frontiers in Bioengineering and Biotechnology, 3, 148. https:\/\/doi.org\/10.3389\/fbioe.2015.00148","journal-title":"Frontiers in Bioengineering and Biotechnology"},{"key":"5481_CR3","doi-asserted-by":"publisher","first-page":"352","DOI":"10.3390\/molecules27185885","volume":"204","author":"M Hamid","year":"2022","unstructured":"Hamid, M., Khan, A. A., & Wani, S. A. (2022). Cold-active enzymes: A biotechnological perspective. International Journal of Biological Macromolecules, 204, 352\u2013367. https:\/\/doi.org\/10.3390\/molecules27185885","journal-title":"International Journal of Biological Macromolecules"},{"issue":"7","key":"5481_CR4","doi-asserted-by":"publisher","first-page":"623","DOI":"10.1016\/j.tibtech.2018.12.007","volume":"37","author":"T Collins","year":"2019","unstructured":"Collins, T., Gerday, C., & Feller, G. (2019). Cold-active enzymes: From fundamentals to biotechnology. Trends in Biotechnology, 37(7), 623\u2013637. https:\/\/doi.org\/10.1016\/j.tibtech.2018.12.007","journal-title":"Trends in Biotechnology"},{"key":"5481_CR5","unstructured":"Future Market Insights. (2024). Protease market size & demand 2024\u20132034. Available from: https:\/\/www.futuremarketinsights.com\/reports\/protease-market. Accessed 25 July 2025."},{"key":"5481_CR6","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s11274-021-03036-z","volume":"37","author":"F Matkawala","year":"2021","unstructured":"Matkawala, F., Nighojkar, S., Kumar, A., & Nighojkar, A. (2021). Microbial alkaline Serine proteases: production, properties and applications. World Journal of Microbiology and Biotechnology, 37, 1\u201312. https:\/\/doi.org\/10.1007\/s11274-021-03036-z","journal-title":"World Journal of Microbiology and Biotechnology"},{"issue":"2","key":"5481_CR7","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1089\/ind.2018.0032","volume":"15","author":"M Sharma","year":"2019","unstructured":"Sharma, M., Gat, Y., Arya, S., Kumar, V., Panghal, A., & Kumar, A. (2019). A review on microbial alkaline protease: An essential tool for various industrial approaches. Industrial Biotechnology, 15(2), 69\u201378. https:\/\/doi.org\/10.1089\/ind.2018.0032","journal-title":"Industrial Biotechnology"},{"key":"5481_CR8","doi-asserted-by":"publisher","unstructured":"Liu, Y., Zhang, N., Ma, J., Zhou, Y., Wei, Q., Tian, C., \u2026 Zhang, S. (2023). Advances in cold-adapted enzymes derived from microorganisms. Frontiers in Microbiology, 14, 1152847. https:\/\/doi.org\/10.3389\/fmicb.2023.1152847","DOI":"10.3389\/fmicb.2023.1152847"},{"issue":"1","key":"5481_CR9","doi-asserted-by":"publisher","first-page":"8873948","DOI":"10.1155\/2023\/8873948","volume":"2023","author":"F Sameni","year":"2023","unstructured":"Sameni, F., Hajikhani, B., Hashemi, A., Owlia, P., Niakan, M., & Dadashi, M. (2023). The relationship between the biofilm genes and antibiotic resistance in Stenotrophomonas maltophilia. International Journal of Microbiology, 2023(1), 8873948. https:\/\/doi.org\/10.1155\/2023\/8873948","journal-title":"International Journal of Microbiology"},{"issue":"7","key":"5481_CR10","doi-asserted-by":"publisher","first-page":"514","DOI":"10.1038\/nrmicro2163","volume":"7","author":"RP Ryan","year":"2009","unstructured":"Ryan, R. P., Monchy, S., Cardinale, M., Taghavi, S., Crossman, L., Avison, M. B., & Dow, J. M. (2009). The versatility and adaptation of bacteria from the genus Stenotrophomonas. Nature Reviews Microbiology, 7(7), 514\u2013525. https:\/\/doi.org\/10.1038\/nrmicro2163","journal-title":"Nature Reviews Microbiology"},{"key":"5481_CR11","doi-asserted-by":"publisher","first-page":"103186","DOI":"10.1016\/j.bcab.2024.103186","volume":"58","author":"MN Uddin","year":"2024","unstructured":"Uddin, M. N., Akter, Y., Chowdhury, M. A. B., Shimizu, K., & Marzan, L. W. (2024). Exploring alkaline Serine protease production and characterization in proteolytic bacteria Stenotrophomonas maltophilia: Insights from real-time PCR and fermentation techniques. Biocatalysis and Agricultural Biotechnology, 58, 103186. https:\/\/doi.org\/10.1016\/j.bcab.2024.103186","journal-title":"Biocatalysis and Agricultural Biotechnology"},{"issue":"3","key":"5481_CR12","doi-asserted-by":"publisher","first-page":"92","DOI":"10.3390\/pathogens8030092","volume":"8","author":"K Molloy","year":"2019","unstructured":"Molloy, K., Smith, S. G., Cagney, G., Dillon, E. T., Greene, C. M., & McElvaney, N. G. (2019). Characterisation of the major extracellular proteases of Stenotrophomonas maltophilia and their effects on pulmonary antiproteases. Pathogens, 8(3), 92. https:\/\/doi.org\/10.3390\/pathogens8030092","journal-title":"Pathogens"},{"issue":"6","key":"5481_CR13","doi-asserted-by":"publisher","first-page":"614","DOI":"10.1016\/j.jbiosc.2015.11.011","volume":"121","author":"U Jankiewicz","year":"2016","unstructured":"Jankiewicz, U., Larkowska, E., & Brzezinska, M. S. (2016). Production, characterization, gene cloning, and nematocidal activity of the extracellular protease from Stenotrophomonas maltophilia N4. Journal of Bioscience and Bioengineering, 121(6), 614\u2013618. https:\/\/doi.org\/10.1016\/j.jbiosc.2015.11.011","journal-title":"Journal of Bioscience and Bioengineering"},{"key":"5481_CR14","doi-asserted-by":"publisher","unstructured":"Ribitsch, D., Heumann, S., Karl, W., Gerlach, J., Leber, R., Birner-Gruenberger, R.,\u2026 Schwab, H. (2012). Extracellular serine proteases from Stenotrophomonas maltophilia: screening, isolation and heterologous expression in E. coli. Journal of Biotechnology, 157(1), 140\u2013147. https:\/\/doi.org\/10.1016\/j.jbiotec.2011.09.025","DOI":"10.1016\/j.jbiotec.2011.09.025"},{"issue":"13","key":"5481_CR15","doi-asserted-by":"publisher","first-page":"11042","DOI":"10.1074\/jbc.M109525200","volume":"277","author":"S Windhorst","year":"2002","unstructured":"Windhorst, S., Frank, E., Georgieva, D. N., Genov, N., Buck, F., Borowski, P., & Weber, W. (2002). The major extracellular protease of the nosocomial pathogen Stenotrophomonas maltophilia: Characterization of the protein and molecular cloning of the gene. Journal of Biological Chemistry, 277(13), 11042\u201311049. https:\/\/doi.org\/10.1074\/jbc.M109525200","journal-title":"Journal of Biological Chemistry"},{"issue":"5","key":"5481_CR16","first-page":"444","volume":"58","author":"B Shahnavaz","year":"2021","unstructured":"Shahnavaz, B., Nikbakhti, R., & Asoodeh, A. (2021). Purification and characterization of an extracellular alkaline cold-adapted Serine metalo-protease from the cold tolerant bacterium, Stenotrophomonas sp. BTR88. Indian Journal of Biochemistry and Biophysics (IJBB), 58(5), 444\u2013450.","journal-title":"Indian Journal of Biochemistry and Biophysics (IJBB)"},{"issue":"11","key":"5481_CR17","doi-asserted-by":"publisher","first-page":"1294","DOI":"10.1139\/W09-089","volume":"55","author":"M Kuddus","year":"2009","unstructured":"Kuddus, M., & Ramteke, P. W. (2009). Cold-active extracellular alkaline protease from an alkaliphilic Stenotrophomonas maltophilia: Production of enzyme and its industrial applications. Canadian Journal of Microbiology, 55(11), 1294\u20131301. https:\/\/doi.org\/10.1139\/W09-089","journal-title":"Canadian Journal of Microbiology"},{"issue":"4","key":"5481_CR18","doi-asserted-by":"publisher","first-page":"319","DOI":"10.1007\/s00300-004-0673-6","volume":"28","author":"S Vazquez","year":"2005","unstructured":"Vazquez, S., Ruberto, L., & Mac Cormack, W. (2005). Properties of extracellular proteases from three psychrotolerant Stenotrophomonas maltophilia isolated from Antarctic soil. Polar Biology, 28(4), 319\u2013325. https:\/\/doi.org\/10.1007\/s00300-004-0673-6","journal-title":"Polar Biology"},{"issue":"3","key":"5481_CR19","doi-asserted-by":"publisher","first-page":"457","DOI":"10.1007\/s43393-022-00130-7","volume":"3","author":"K Zhao","year":"2023","unstructured":"Zhao, K., Liu, H., Song, W., Wu, J., Gao, C., Guo, L., & Chen, X. (2023). Combinatorial mutagenesis of Bacillus amyloliquefaciens for efficient production of protease. Systems Microbiology and Biomanufacturing, 3(3), 457\u2013468. https:\/\/doi.org\/10.1007\/s43393-022-00130-7","journal-title":"Systems Microbiology and Biomanufacturing"},{"key":"5481_CR20","doi-asserted-by":"publisher","unstructured":"Wang, Q., Ji, F., Wang, J., Jiang, B., Li, L., An, L., \u2026 Bao, Y. (2016). Characterization of a salt-activated protease with temperature-dependent secretion in Stenotrophomonas maltophilia FF11 isolated from frozen Antarctic krill. Journal of Industrial Microbiology and Biotechnology, 43(6), 829\u2013840. https:\/\/doi.org\/10.1007\/s10295-016-1749-3","DOI":"10.1007\/s10295-016-1749-3"},{"key":"5481_CR21","first-page":"512","volume":"10","author":"K Tamura","year":"1993","unstructured":"Tamura, K., & Nei, M. (1993). Estimation of the number of nucleotide substitutions in the control region of mitochondrial DNA in humans and chimpanzees. Molecular Biology and Evolution, 10, 512\u2013526.","journal-title":"Molecular Biology and Evolution"},{"key":"5481_CR22","doi-asserted-by":"publisher","first-page":"783","DOI":"10.1111\/j.1558-5646.1985.tb00420.x","volume":"39","author":"J Felsenstein","year":"1985","unstructured":"Felsenstein, J. (1985). Confidence limits on phylogenies: An approach using the bootstrap. Evolution, 39, 783\u2013791.","journal-title":"Evolution"},{"issue":"6","key":"5481_CR23","doi-asserted-by":"publisher","first-page":"1547","DOI":"10.1093\/molbev\/msy096","volume":"35","author":"S Kumar","year":"2018","unstructured":"Kumar, S., Stecher, G., Li, M., Knyaz, C., & Tamura, K. (2018). MEGA X: Molecular evolutionary genetics analysis across computing platforms. Molecular Biology and Evolution, 35(6), 1547\u20131549. https:\/\/doi.org\/10.1093\/molbev\/msy096","journal-title":"Molecular Biology and Evolution"},{"issue":"3","key":"5481_CR24","doi-asserted-by":"publisher","first-page":"e0283677","DOI":"10.1371\/journal.pone.0283677","volume":"18","author":"H Mushtaq","year":"2023","unstructured":"Mushtaq, H., Ganai, S. A., Jehangir, A., Ganai, B. A., & Dar, R. (2023). Molecular and functional characterization of protease from psychrotrophic Bacillus sp. HM49 in North-western himalaya. Plos One, 18(3), e0283677. https:\/\/doi.org\/10.1371\/journal.pone.0283677","journal-title":"Plos One"},{"issue":"7","key":"5481_CR25","doi-asserted-by":"publisher","first-page":"809","DOI":"10.5897\/AJMR10.806","volume":"5","author":"M Kuddus","year":"2011","unstructured":"Kuddus, M., & Ramteke, P. W. (2011). Production optimization of an extracellular cold-active alkaline protease from Stenotrophomonas maltophilia MTCC 7528 and its application in detergent industry. African Journal of Microbiology Research, 5(7), 809\u2013816. https:\/\/doi.org\/10.5897\/AJMR10.806","journal-title":"African Journal of Microbiology Research"},{"issue":"03","key":"5481_CR26","first-page":"107","volume":"01","author":"KS Naidu","year":"2011","unstructured":"Naidu, K. S. (2011). Characterization and purification of protease enzyme. Journal of Applied Pharmaceutical Science, 01(03), 107\u2013112.","journal-title":"Journal of Applied Pharmaceutical Science"},{"key":"5481_CR27","doi-asserted-by":"publisher","first-page":"1227","DOI":"10.1016\/j.ijbiomac.2018.10.139","volume":"121","author":"H Rekik","year":"2019","unstructured":"Rekik, H., Jaouadi, N. Z., Gargouri, F., Bejar, W., Frikha, F., Jmal, N., Bejar, S., & Jaouadi, B. (2019). Production, purification and biochemical characterization of a novel detergent-stable Serine alkaline protease from Bacillus safensis strain RH12. International Journal of Biological Macromolecules, 121, 1227\u20131239. https:\/\/doi.org\/10.1016\/j.ijbiomac.2018.10.139","journal-title":"International Journal of Biological Macromolecules"},{"issue":"1\u20132","key":"5481_CR28","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","volume":"72","author":"MM Bradford","year":"1976","unstructured":"Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72(1\u20132), 248\u2013254. https:\/\/doi.org\/10.1016\/0003-2697(76)90527-3","journal-title":"Analytical Biochemistry"},{"key":"5481_CR29","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.pep.2014.11.002","volume":"107","author":"SR Waghmare","year":"2015","unstructured":"Waghmare, S. R., Gurav, A. A., Mali, S. A., Nadaf, N. H., Jadhav, D. B., & Sonawane, K. D. (2015). Purification and characterization of novel organic solvent tolerant 98\u00a0kDa alkaline protease from isolated Stenotrophomonas maltophilia strain SK. Protein Expression and Purification, 107, 1\u20136. https:\/\/doi.org\/10.1016\/j.pep.2014.11.002","journal-title":"Protein Expression and Purification"},{"key":"5481_CR30","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/j.foodchem.2016.08.064","volume":"217","author":"A Mageswari","year":"2017","unstructured":"Mageswari, A., Subramanian, P., Chandrasekaran, S., Karthikeyan, S., & Gothandam, K. M. (2017). Systematic functional analysis and application of a cold-active Serine protease from a novel Chryseobacterium Sp. Food Chemistry, 217, 18\u201327. https:\/\/doi.org\/10.1016\/j.foodchem.2016.08.064","journal-title":"Food Chemistry"},{"issue":"5259","key":"5481_CR31","doi-asserted-by":"publisher","first-page":"680","DOI":"10.1038\/227680a0","volume":"227","author":"UK Laemmli","year":"1970","unstructured":"Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680\u2013685. https:\/\/doi.org\/10.1038\/227680a0","journal-title":"Nature"},{"key":"5481_CR32","doi-asserted-by":"publisher","first-page":"272","DOI":"10.1016\/j.ijbiomac.2016.12.035","volume":"96","author":"A Hammami","year":"2017","unstructured":"Hammami, A., Hamdi, M., Abdelhedi, O., Jridi, M., Nasri, M., & Bayoudh, A. (2017). Surfactant-and oxidant-stable alkaline proteases from Bacillus invictae: Characterization and potential applications in Chitin extraction and as a detergent additive. International Journal of Biological Macromolecules, 96, 272\u2013281. https:\/\/doi.org\/10.1016\/j.ijbiomac.2016.12.035","journal-title":"International Journal of Biological Macromolecules"},{"issue":"6","key":"5481_CR33","doi-asserted-by":"publisher","first-page":"1248","DOI":"10.1016\/j.procbio.2011.02.012","volume":"46","author":"K Jellouli","year":"2011","unstructured":"Jellouli, K., Ghorbel-Bellaaj, O., Ayed, H. B., Manni, L., Agrebi, R., & Nasri, M. (2011). Alkaline-protease from Bacillus licheniformis MP1: purification, characterization and potential application as a detergent additive and for shrimp waste deproteinization. Process Biochemistry, 46(6), 1248\u20131256. https:\/\/doi.org\/10.1016\/j.procbio.2011.02.012","journal-title":"Process Biochemistry"},{"key":"5481_CR34","doi-asserted-by":"publisher","first-page":"1071","DOI":"10.1007\/s11274-011-0905-1","volume":"28","author":"I Saba","year":"2012","unstructured":"Saba, I., Qazi, P. H., Rather, S. A., Dar, R. A., Qadri, Q. A., Ahmad, N., & Shawl, S. (2012). Purification and characterization of a cold active alkaline protease from Stenotrophomonas sp., isolated from Kashmir, India. World Journal of Microbiology and Biotechnology, 28, 1071\u20131079. https:\/\/doi.org\/10.1007\/s11274-011-0905-1","journal-title":"World Journal of Microbiology and Biotechnology"},{"key":"5481_CR35","doi-asserted-by":"publisher","first-page":"1033","DOI":"10.1016\/j.ijbiomac.2018.03.167","volume":"114","author":"R Hadjidj","year":"2018","unstructured":"Hadjidj, R., Badis, A., Mechri, S., Eddouaouda, K., Khelouia, L., Annane, R., & Jaouadi, B. (2018). Purification, biochemical, and molecular characterization of novel protease from Bacillus licheniformis strain K7A. International Journal of Biological Macromolecules, 114, 1033\u20131048. https:\/\/doi.org\/10.1016\/j.ijbiomac.2018.03.167","journal-title":"International Journal of Biological Macromolecules"},{"issue":"2","key":"5481_CR36","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1016\/j.jgeb.2018.07.003","volume":"16","author":"IK Shaikh","year":"2018","unstructured":"Shaikh, I. K., Dixit, P. P., & Shaikh, T. M. (2018). Purification and characterization of alkaline soda-bleach stable protease from Bacillus sp. APP-07 isolated from laundromat soil. Journal of Genetic Engineering and Biotechnology, 16(2), 273\u2013279. https:\/\/doi.org\/10.1016\/j.jgeb.2018.07.003","journal-title":"Journal of Genetic Engineering and Biotechnology"},{"issue":"4","key":"5481_CR37","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1007\/s12088-023-01115-3","volume":"63","author":"N Arabac\u0131","year":"2023","unstructured":"Arabac\u0131, N., & Karaytu\u011f, T. (2023). Alkaline thermo-and oxidant-stable protease from Bacillus pumilus strain TNP93: Laundry detergent formulations. Indian Journal of Microbiology, 63(4), 575\u2013587. https:\/\/doi.org\/10.1007\/s12088-023-01115-3","journal-title":"Indian Journal of Microbiology"},{"key":"5481_CR38","doi-asserted-by":"publisher","first-page":"3572","DOI":"10.1007\/s10562-020-03268-y","volume":"150","author":"SA Qamar","year":"2020","unstructured":"Qamar, S. A., Asgher, M., & Bilal, M. (2020). Immobilization of alkaline protease from Bacillus brevis using Ca-alginate entrapment strategy for improved catalytic stability, silver recovery, and dehairing potentialities. Catalysis Letters, 150, 3572\u20133583. https:\/\/doi.org\/10.1007\/s10562-020-03268-y","journal-title":"Catalysis Letters"},{"issue":"6","key":"5481_CR39","doi-asserted-by":"publisher","first-page":"45","DOI":"10.11648\/j.fem.20160206.14","volume":"2","author":"BKM Lakshmi","year":"2016","unstructured":"Lakshmi, B. K. M., & Hemalatha, K. P. J. (2016). Eco friendly recovery of silver from used X-ray films by alkaline protease of Bacillus cereus strain S8. Frontiers in Environmental Microbiology, 2(6), 45\u201348. https:\/\/doi.org\/10.11648\/j.fem.20160206.14","journal-title":"Frontiers in Environmental Microbiology"},{"issue":"6","key":"5481_CR40","doi-asserted-by":"publisher","first-page":"876","DOI":"10.1007\/s10930-021-10023-8","volume":"40","author":"SM Keziah","year":"2021","unstructured":"Keziah, S. M., & Devi, C. S. (2021). Fibrinolytic and ACE inhibitory activity of nattokinase extracted from Bacillus subtilis VITMS 2: A strain isolated from fermented milk of Vigna unguiculata. The Protein Journal, 40(6), 876\u2013890. https:\/\/doi.org\/10.1007\/s10930-021-10023-8","journal-title":"The Protein Journal"},{"issue":"6","key":"5481_CR41","doi-asserted-by":"publisher","first-page":"2004","DOI":"10.1007\/s12010-021-03494-z","volume":"193","author":"S Khankari","year":"2021","unstructured":"Khankari, S., Badoei-Dalfard, A., & Karami, Z. (2021). Cross-linked enzyme aggregates of fibrinolytic protease BC1 immobilized on magnetic Chitosan nanoparticles (CLEAs-Fib-mChi): synthesis, purification, and characterization. Applied Biochemistry and Biotechnology, 193(6), 2004\u20132027. https:\/\/doi.org\/10.1007\/s12010-021-03494-z","journal-title":"Applied Biochemistry and Biotechnology"},{"issue":"2","key":"5481_CR42","doi-asserted-by":"publisher","first-page":"327","DOI":"10.4014\/jmb.2008.08010","volume":"31","author":"J Frias","year":"2021","unstructured":"Frias, J., Toubarro, D., Fraga, A., Botelho, C., Teixeira, J., Pedrosa, J., & ve Sim\u00f5es, N. (2021). Purification and characterization of a thrombolytic enzyme produced by a new strain of Bacillus subtilis. Journal of Microbiology and Biotechnology, 31(2), 327. https:\/\/doi.org\/10.4014\/jmb.2008.08010","journal-title":"Journal of Microbiology and Biotechnology"},{"issue":"5","key":"5481_CR43","doi-asserted-by":"publisher","first-page":"157","DOI":"10.2323\/jgam.61.157","volume":"61","author":"MK Narasimhan","year":"2015","unstructured":"Narasimhan, M. K., Chandrasekaran, M., & Rajesh, M. (2015). Fibrinolytic enzyme production by newly isolated Bacillus cereus SRM-001 with enhanced in-vitro blood clot Lysis potential. The Journal of General and Applied Microbiology, 61(5), 157\u2013164. https:\/\/doi.org\/10.2323\/jgam.61.157","journal-title":"The Journal of General and Applied Microbiology"},{"key":"5481_CR44","doi-asserted-by":"publisher","first-page":"793","DOI":"10.1016\/j.ijbiomac.2016.09.048","volume":"94","author":"X Liu","year":"2017","unstructured":"Liu, X., Kopparapu, N. K., Li, Y., Deng, Y., & Zheng, X. (2017). Biochemical characterization of a novel fibrinolytic enzyme from Cordyceps militaris. International Journal of Biological Macromolecules, 94, 793\u2013801. https:\/\/doi.org\/10.1016\/j.ijbiomac.2016.09.048","journal-title":"International Journal of Biological Macromolecules"},{"issue":"2","key":"5481_CR45","doi-asserted-by":"publisher","first-page":"e0191740","DOI":"10.1371\/journal.pone.0191740","volume":"13","author":"HJ Park","year":"2018","unstructured":"Park, H. J., Lee, C. W., Kim, D., Do, H., Han, S. J., Kim, J. E., & Yim, J. H. (2018). Crystal structure of a cold-active protease (Pro21717) from the psychrophilic bacterium,Pseudoalteromonas Arctica PAMC 21717, at 1.4 \u00c5 resolution: Structural adaptations to cold and functional analysis of a laundry detergent enzyme. PLoS One, 13(2), e0191740. https:\/\/doi.org\/10.1371\/journal.pone.0191740","journal-title":"PLoS One"},{"key":"5481_CR46","doi-asserted-by":"publisher","unstructured":"Lich, N. Q., Thao, T. T. P., & Huy, N. D. (2022). Characterization of extracellular protease from Stenotrophomonas rhizophila MT1 isolated from aquaculture sludge waste. Applied Ecology & Environmental Research, 20(3). https:\/\/doi.org\/10.15666\/aeer\/2003_24092423","DOI":"10.15666\/aeer\/2003_24092423"},{"issue":"6","key":"5481_CR47","doi-asserted-by":"publisher","first-page":"3321","DOI":"10.1128\/AEM.70.6.3321-3328.2004","volume":"70","author":"AL Huston","year":"2004","unstructured":"Huston, A. L., Methe, B., & Deming, J. W. (2004). Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia Psychrerythraea strain 34H. Applied and Environmental Microbiology, 70(6), 3321\u20133328. https:\/\/doi.org\/10.1128\/AEM.70.6.3321-3328.2004","journal-title":"Applied and Environmental Microbiology"},{"key":"5481_CR48","doi-asserted-by":"publisher","unstructured":"Furhan, J., Awasthi, P., ve, & Sharma, S. (2019). Biochemical characterization and homology modelling of cold-active alkophilic protease from Northwestern Himalayas and its application in detergent industry. Biocatalysis and Agricultural Biotechnology, 17, 726\u2013735. https:\/\/doi.org\/10.1016\/j.bcab.2019.01.028","DOI":"10.1016\/j.bcab.2019.01.028"},{"key":"5481_CR49","doi-asserted-by":"publisher","first-page":"935072","DOI":"10.3389\/fmicb.2022.935072","volume":"13","author":"Y Wen","year":"2022","unstructured":"Wen, Y., Qiang, J., Zhou, G., Zhang, X., Wang, L., & Shi, Y. (2022). Characterization of redox and salinity-tolerant alkaline protease from Bacillus halotolerans strain DS5. Frontiers in Microbiology, 13, 935072. https:\/\/doi.org\/10.3389\/fmicb.2022.935072","journal-title":"Frontiers in Microbiology"},{"key":"5481_CR50","doi-asserted-by":"publisher","first-page":"176","DOI":"10.1007\/s12257-017-0495-3","volume":"23","author":"JB Si","year":"2018","unstructured":"Si, J. B., Jang, E. J., Charalampopoulos, D., & Wee, Y. J. (2018). Purification and characterization of microbial protease produced extracellularly from Bacillus subtilis FBL-1. Biotechnology and Bioprocess Engineering, 23, 176\u2013182. https:\/\/doi.org\/10.1007\/s12257-017-0495-3","journal-title":"Biotechnology and Bioprocess Engineering"},{"issue":"8","key":"5481_CR51","doi-asserted-by":"publisher","first-page":"934","DOI":"10.1139\/W09-045","volume":"55","author":"X Huang","year":"2009","unstructured":"Huang, X., Liu, J., Ding, J., He, Q., Xiong, R., & Zhang, K. (2009). The investigation of nematocidal activity in Stenotrophomonas maltophilia G2 and characterization of a novel virulence Serine protease. Canadian Journal of Microbiology, 55(8), 934\u2013942. https:\/\/doi.org\/10.1139\/W09-045","journal-title":"Canadian Journal of Microbiology"},{"issue":"6","key":"5481_CR52","doi-asserted-by":"publisher","first-page":"5774","DOI":"10.3390\/ijms24065774","volume":"24","author":"H Tarek","year":"2023","unstructured":"Tarek, H., Nam, K. B., Kim, Y. K., Suchi, S. A., & Yoo, J. C. (2023). Biochemical characterization and application of a detergent stable, antimicrobial and antibiofilm potential protease from Bacillus siamensis. International Journal of Molecular Sciences, 24(6), 5774. https:\/\/doi.org\/10.3390\/ijms24065774","journal-title":"International Journal of Molecular Sciences"},{"key":"5481_CR53","doi-asserted-by":"publisher","unstructured":"Durga, V., & Ahmad, S. S. (2022). Low-level express\u0131on of enzyme from marine fungi species for dye decolorization. Journal of Pharmaceutical Negative Results, 13. https:\/\/doi.org\/10.9734\/jabb\/2023\/v26i1612","DOI":"10.9734\/jabb\/2023\/v26i1612"},{"issue":"2","key":"5481_CR54","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1007\/s11756-022-01281-7","volume":"78","author":"A Varol","year":"2023","unstructured":"Varol, A., Albayrak, S., Ozkan, H., Demir, Y., Taskin, M., & Adiguzel, A. (2023). Production, purification and characterization of novel fibrinolytic enzyme from Bacillus atrophaeus V4. Biologia, 78(2), 591\u2013600. https:\/\/doi.org\/10.1007\/s11756-022-01281-7","journal-title":"Biologia"},{"issue":"2","key":"5481_CR55","doi-asserted-by":"publisher","first-page":"124","DOI":"10.1080\/10242422.2018.1504925","volume":"37","author":"K Taneja","year":"2019","unstructured":"Taneja, K., Kumar Bajaj, B., Kumar, S., & Dilbaghi, N. (2019). Process optimization for production and purification of novel fibrinolytic enzyme from Stenotrophomonas sp. KG-16-3. Biocatalysis and Biotransformation, 37(2), 124\u2013138. https:\/\/doi.org\/10.1080\/10242422.2018.1504925","journal-title":"Biocatalysis and Biotransformation"},{"issue":"1","key":"5481_CR56","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1134\/S0003683821010087","volume":"57","author":"J Furhan","year":"2021","unstructured":"Furhan, J., & Nissar, J. (2021). Cold-adapted Serine metalloprotease from Serratia DLCP2: purification, characterization and industrial potential. Applied Biochemistry and Microbiology, 57(1), 40\u201347. https:\/\/doi.org\/10.1134\/S0003683821010087","journal-title":"Applied Biochemistry and Microbiology"},{"issue":"1","key":"5481_CR57","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1111\/j.1574-6968.2000.tb09360.x","volume":"192","author":"MA Lee","year":"2000","unstructured":"Lee, M. A., & Liu, Y. (2000). Sequencing and characterization of a novel Serine metalloprotease from Burkholderia Pseudomallei. FEMS Microbiology Letters, 192(1), 67\u201372. https:\/\/doi.org\/10.1111\/j.1574-6968.2000.tb09360.x","journal-title":"FEMS Microbiology Letters"},{"key":"5481_CR58","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s40643-014-0008-6","volume":"1","author":"FM Olajuyigbe","year":"2014","unstructured":"Olajuyigbe, F. M., & Falade, A. M. (2014). Purification and partial characterization of Serine alkaline metalloprotease from Bacillus brevis MWB-01. Bioresources and Bioprocessing, 1, 1\u201310. https:\/\/doi.org\/10.1186\/s40643-014-0008-6","journal-title":"Bioresources and Bioprocessing"},{"key":"5481_CR59","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s13205-018-1133-2","volume":"8","author":"MQ Lam","year":"2018","unstructured":"Lam, M. Q., Nik Mut, N. N., Thevarajoo, S., Chen, S. J., Selvaratnam, C., Hussin, H., Jamaluddin, H., & Chong, C. S. (2018). Characterization of detergent compatible protease from halophilic Virgibacillus sp. CD6. 3 Biotech, 8, 1\u20139. https:\/\/doi.org\/10.1007\/s13205-018-1133-2","journal-title":"3 Biotech"},{"key":"5481_CR60","doi-asserted-by":"crossref","unstructured":"Zhang, H., Mu, H., Mo, Q., Sun, T., Liu, Y., Xu, M., \u2026 Lu, F. (2016). Gene cloning,expression and characterization of a novel cold-adapted protease from Planococcus sp. Journal of Molecular Catalysis B: Enzymatic, 130, 1\u20138. http:\/\/dx.doi.org\/10.1016\/j.molcatb.2016.04.002","DOI":"10.1016\/j.molcatb.2016.04.002"},{"key":"5481_CR61","doi-asserted-by":"publisher","unstructured":"Xiuqin, C., Chunxia, B., Weiqi, S., Wei, Z., Jie, S., Yumei, D., \u2026 Zhiyong, Y. (2013).Purification and stability characteristics of an extracellular alkaline serine protease from a newly isolated Stenotrophomonas maltophilia strain D2. African Journal of Microbiology Research, 7(33), 4244\u20134250. https:\/\/doi.org\/10.5897\/AJMR2013.2547","DOI":"10.5897\/AJMR2013.2547"},{"key":"5481_CR62","first-page":"448","volume":"17","author":"S Guleria","year":"2018","unstructured":"Guleria, S., Walia, A., Chauhan, A., & Shirkot, C. K. (2018). Production and eco-friendly application of alkaline protease from Bacillus amyloliquefaciens sp1. Indian J Biotechnol, 17, 448\u2013458.","journal-title":"Indian J Biotechnol"},{"key":"5481_CR63","doi-asserted-by":"publisher","unstructured":"Liya, S. M., Umesh, M., Nag, A., Chinnathambi, A., Alharbi, S. A., Jhanani, G. K.,\u2026 Brindhadevi, K. (2023). Optimized production of keratinolytic proteases from Bacillus tropicus LS27 and its application as a sustainable alternative for dehairing, destaining and metal recovery. Environmental research, 221, 115283. https:\/\/doi.org\/10.1016\/j.envres.2023.115283","DOI":"10.1016\/j.envres.2023.115283"},{"issue":"3","key":"5481_CR64","first-page":"349","volume":"25","author":"N Nakibo\u011flu","year":"2001","unstructured":"Nakibo\u011flu, N., Toscali, D., & Ya\u015fa, \u0130. (2001). Silver recovery from waste photographic films by using enzymatic method. Turkish Journal of Chemistry, 25(3), 349\u2013353.","journal-title":"Turkish Journal of Chemistry"},{"issue":"1","key":"5481_CR65","doi-asserted-by":"publisher","first-page":"98","DOI":"10.1186\/s12934-025-02706-z","volume":"24","author":"MA Abdella","year":"2025","unstructured":"Abdella, M. A., & Ahmed, S. A. (2025). Stable protease from Bacillus licheniformis-MA1 strain: Statistical production optimization, kinetic and thermodynamic characterization, and application in silver recovery from used X-ray films. Microbial Cell Factories, 24(1), 98. https:\/\/doi.org\/10.1186\/s12934-025-02706-z","journal-title":"Microbial Cell Factories"},{"issue":"26","key":"5481_CR66","doi-asserted-by":"publisher","first-page":"1413","DOI":"10.5897\/AJB2016.15340","volume":"15","author":"AH Al-Abdalall","year":"2016","unstructured":"Al-Abdalall, A. H., & Al-Khaldi, E. M. (2016). Recovery of silver from used X-ray film using alkaline protease from Bacillus subtilis sub sp. subtilis. African Journal of Biotechnology, 15(26), 1413\u20131416. https:\/\/doi.org\/10.5897\/AJB2016.15340","journal-title":"African Journal of Biotechnology"},{"issue":"7","key":"5481_CR67","doi-asserted-by":"publisher","first-page":"637","DOI":"10.3390\/fermentation9070637","volume":"9","author":"E Kotb","year":"2023","unstructured":"Kotb, E., Alabdalall, A. H., Alsayed, M. A., Alghamdi, A. I., Alkhaldi, E., AbdulAzeez, S., & Borgio, J. F. (2023). Isolation, screening, and identification of alkaline protease-producing bacteria and application of the most potent enzyme from Bacillus sp. Mar64. Fermentation, 9(7), 637. https:\/\/doi.org\/10.3390\/fermentation9070637","journal-title":"Fermentation"},{"issue":"8","key":"5481_CR68","first-page":"569","volume":"50","author":"AP Pathak","year":"2012","unstructured":"Pathak, A. P., & Deshmukh, K. B. (2012). Alkaline protease production, extraction and characterization from alkaliphilic Bacillus licheniformis KBDL4: A Lonar soda lake isolate. Indian Journal of Experimental Biology, 50(8), 569\u2013576.","journal-title":"Indian Journal of Experimental Biology"},{"issue":"2","key":"5481_CR69","doi-asserted-by":"publisher","first-page":"755","DOI":"10.3390\/biology2020755","volume":"2","author":"S Joshi","year":"2013","unstructured":"Joshi, S., & Satyanarayana, T. (2013). Biotechnology of cold-active proteases. Biology, 2(2), 755\u2013783. https:\/\/doi.org\/10.3390\/biology2020755","journal-title":"Biology"},{"key":"5481_CR70","doi-asserted-by":"publisher","first-page":"115403","DOI":"10.1016\/j.indcrop.2022.115403","volume":"187","author":"N Reddy","year":"2022","unstructured":"Reddy, N., Deekonda, V., Seshagiri, S., Reddy, R., & Gangula, A. K. (2022). Production, characterization and applications of proteases produced by Bacillus licheniformis, acinetobacter Pittii and Aspergillus Niger using Neem seed oil cake as the substrate. Industrial Crops and Products, 187, 115403. https:\/\/doi.org\/10.1016\/j.indcrop.2022.115403","journal-title":"Industrial Crops and Products"},{"key":"5481_CR71","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ejbt.2016.01.002","volume":"20","author":"P Vijayaraghavan","year":"2016","unstructured":"Vijayaraghavan, P., Vincent, S. G. P., Arasu, M. V., & Al-Dhabi, N. A. (2016). Bioconversion of agro-industrial wastes for the production of fibrinolytic enzyme from Bacillus halodurans IND18: Purification and biochemical characterization. Electronic Journal of Biotechnology, 20, 1\u20138. https:\/\/doi.org\/10.1016\/j.ejbt.2016.01.002","journal-title":"Electronic Journal of Biotechnology"},{"issue":"2","key":"5481_CR72","doi-asserted-by":"publisher","first-page":"147","DOI":"10.11598\/btb.2023.30.2.1765","volume":"30","author":"A Ainutajriani","year":"2023","unstructured":"Ainutajriani, A., Darmawati, S., Zilda, D. S., Afriansyah, M. A., Saptaningtyas, R., & Ethica, S. N. (2023). Production optimization, partial purification, and thrombolytic activity evaluation of protease of Bacillus cereus HSFI-10. Biotropia, 30(2), 147\u2013157. https:\/\/doi.org\/10.11598\/btb.2023.30.2.1765","journal-title":"Biotropia"},{"issue":"2","key":"5481_CR73","doi-asserted-by":"publisher","first-page":"135","DOI":"10.3329\/dujps.v15i2.30926","volume":"15","author":"MA uz Zaman","year":"2016","unstructured":"uz Zaman, M. A., Al Mamun, M. A., Khan, S. N., Hoq, M. M., & Mazid, M. A. (2016). Partial purification of alkaline protease as thrombolytic agent from mutant strain Bacillus licheniformis EMS250-O-1. Dhaka University Journal of Pharmaceutical Sciences, 15(2), 135\u2013141. https:\/\/doi.org\/10.3329\/dujps.v15i2.30926","journal-title":"Dhaka University Journal of Pharmaceutical Sciences"},{"issue":"9","key":"5481_CR74","first-page":"75","volume":"10","author":"S G\u00fcrk\u00f6k","year":"2019","unstructured":"G\u00fcrk\u00f6k, S. (2019). Microbial enzymes in detergents: A review. Int J Sci Eng Res, 10(9), 75\u201381.","journal-title":"Int J Sci Eng Res"},{"key":"5481_CR75","unstructured":"Zhang, R., Sun, Y., Hu, C., Shen, R., Liu, X., Xiao, Q., \u2026 Fu, C. (2025). Biosynthesis of keratinase from Stenotrophomonas maltophilia Wu2 from poultry and its effect on poultry feather waste bioutilization, washing and dehairing. Journal of Biotech Research, 20, 176\u2013191."},{"issue":"10","key":"5481_CR76","first-page":"24","volume":"131","author":"PH Nielsen","year":"2005","unstructured":"Nielsen, P. H. (2005). Life cycle assessment supports cold-wash enzymes. S\u00d6FW-journal, 131(10), 24\u201326.","journal-title":"S\u00d6FW-journal"},{"issue":"5","key":"5481_CR77","doi-asserted-by":"publisher","first-page":"3271","DOI":"10.1007\/s12010-024-05147-3","volume":"197","author":"AS Silva","year":"2025","unstructured":"Silva, A. S., Neves, K. M., Freitas, R. F., das Chagas, T. P., Salay, L. C., da Silva, E. G. P., & da Costa, A. M. (2025). Valorization of cocoa and Peach-Palm wastes for the production of amylases by pleurotus pulmonarius CCB19 and its application as an additive in commercial detergents. Applied Biochemistry and Biotechnology, 197(5), 3271\u20133294. https:\/\/doi.org\/10.1007\/s12010-024-05147-3","journal-title":"Applied Biochemistry and Biotechnology"}],"container-title":["Applied Biochemistry and Biotechnology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12010-025-05481-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12010-025-05481-0","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12010-025-05481-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,18]],"date-time":"2026-02-18T06:54:57Z","timestamp":1771397697000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s12010-025-05481-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12,11]]},"references-count":77,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2026,2]]}},"alternative-id":["5481"],"URL":"https:\/\/doi.org\/10.1007\/s12010-025-05481-0","relation":{},"ISSN":["0273-2289","1559-0291"],"issn-type":[{"value":"0273-2289","type":"print"},{"value":"1559-0291","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,12,11]]},"assertion":[{"value":"19 November 2025","order":1,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 December 2025","order":2,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Ethical approval for the use of blood in this study was obtained from the Research Ethics Committee of \u00c7ukurova University Medical Faculty (approval date: December 8th, 2023; approval number: 139\/31). Written informed consent was obtained from the donor who provided the blood sample used in the analysis.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics Approval and Consent to Participate"}},{"value":"The authors approved the final version of the manuscript submitted for publication.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for Publication"}},{"value":"The authors declare no conflict of interest.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}