[1] Xu, J., Wang, X., Zhao, X., Cao, H., Wang, Y., Xie, N., Li, X., Pang, X., Lv, J., & Zhang, S. (2024). Evaluation of UHT milk spoilage caused by proteases from psychrophilic bacteria based on peptidomics. Food Chemistry: X, 24, 102059. https://doi.org/10.1016/j.fochx.2024.102059
[2] D’Incecco, P., Rosi, V., Fortina, M. G., Sindaco, M., Ricci, G., & Pellegrino, L. (2022). Biochemical, microbiological, and structural evaluations to early detect age gelation of milk caused by proteolytic activity of Pseudomonas fluorescens. European Food Research and Technology, 248(5), 2097–2107. https://doi.org/10.1007/s00217-022-04033-8
[3] Ajmal, M., Nadeem, M., Gulzar, N., Ashraf, M., & Batool, M. (2025). Pasteurized and ultrahigh-temperature-treated milk. In A. Gomes da Cruz, T. Colombo Pimentel, E. A. Esmerino, & S. Verruck (Eds.), Dairy foods processing. Methods and protocols in food science. Humana. https://doi.org/10.1007/978-1-0716-4144-6
[4] Maier, C., Huptas, C., von Neubeck, M., Scherer, S., Wenning, M., & Lücking, G. (2020). Genetic organization of the AprX-lipA2 operon affects the proteolytic potential of Pseudomonas species in milk. Frontiers in Microbiology, 11, 1190. https://doi.org/10.3389/fmicb.2020.01190
[5] D’Incecco, P., Brasca, M., Rosi, V., Morandi, S., Ferranti, P., Picariello, G., & Pellegrino, L. (2019). Bacterial proteolysis of casein leading to UHT milk gelation: An applicative study. Food Chemistry, 292, 217–226. https://doi.org/10.1016/j.foodchem.2019.04.066
[6] Aguilera-Toro, M., Nielsen, S. D.-H., Kragh, M. L., Xiao, Y., Hansen, L. T., Rauh, V., Wiking, L., Poulsen, N. A., & Larsen, L. B. (2023). Peptidomic fingerprints of stored UHT milk inoculated with protease extracts from different Pseudomonas strains relative to AprX expression and visible spoilage. Dairy, 4(1), 83–97. https://doi.org/10.3390/dairy4010005
[7] Maier, T., Schleifer, K., & Wagner, R. (2021). Simultaneous quantification of the most common and proteolytic Pseudomonas species in raw milk by multiplex qPCR. Applied Microbiology and Biotechnology, 105(10), 4075–4089. https://doi.org/10.1007/s00253-021-11109-0
[8] Mangin, I., Corroler, D., Reinhardt, A., & Gueguen, M. (1999). Genetic diversity among dairy lactococcal strains investigated by polymerase chain reaction with three arbitrary primers. Journal of Applied Microbiology, 86(3), 514–520. https://doi.org/10.1046/j.1365-2672.1999.00699.x
[9] Jorgensen, J. H., Carroll, K. C., Funke, G., Pfaller, M. A., Landry, M. L., Richter, S. S., & Warnock, D. W. (Eds.). (2015). Manual of clinical microbiology (11th ed.). ASM Press. https://doi.org/10.1128/9781555817381
[10] Yang, K., Dong, X., Li, J., Wang, Y., Cheng, Y., Zhai, Y., Li, X., Wei, L., Jing, M., & Dou, D. (2021). Type 2 Nep1-like proteins from the biocontrol oomycete Pythium oligandrum suppress Phytophthora capsici infection in Solanaceous plants. Journal of Fungi, 7(7), 496. https://doi.org/10.3390/jof7070496
[11] Zhang, C., Bijl, E., Svensson, B., & Hettinga, K. (2019). The extracellular protease AprX from Pseudomonas and its spoilage potential for UHT milk: A review. Comprehensive Reviews in Food Science and Food Safety, 18(4), 834–852. https://doi.org/10.1111/1541-4337.12452
[12] Aguilera-Toro, M., Kragh, M. L., Thomasen, A. V., Piccini, V., Rauh, V., Xiao, Y., Wiking, L., Poulsen, N. A., Hansen, L. T., & Larsen, L. B. (2023). Proteolytic activity and heat resistance of the protease AprX from Pseudomonas in relation to genotypic characteristics. International Journal of Food Microbiology, 391–393, 110147. https://doi.org/10.1016/j.ijfoodmicro.2023.110147
[13] Zhang, C., Bijl, E., Muis, K. E., & Hettinga, K. (2020). Stability of fat globules in UHT milk during proteolysis by the AprX protease from Pseudomonas fluorescens and by plasmin. Journal of Dairy Science, 103(1), 179–190. https://doi.org/10.3168/jds.2019-17150
[14] MacFaddin, J. F. (2000). Biochemical tests for identification of medical bacteria (3rd ed.). Lippincott Williams & Wilkins.
[15] Wagner, J., Short, K., Catto-Smith, A. G., Cameron, D. J., Bishop, R. F., & Kirkwood, C. D. (2008). Identification and characterisation of Pseudomonas 16S ribosomal DNA from ileal biopsies of children with Crohn’s disease. PLoS ONE, 3(10), e3578. https://doi.org/10.1371/journal.pone.0003578
[16] Ercolini, D., Russo, F., Nasi, A., Ferranti, P., & Villani, F. (2009). Molecular identification of mesophilic and psychrotrophic bacteria from raw cow’s milk. Food Microbiology, 26(2), 228–238. https://doi.org/10.1016/j.fm.2008.09.005
[17] Paludetti, L. F., Kelly, A. L., & Gleeson, D. (2020). Effect of thermoresistant protease of Pseudomonas fluorescens on rennet coagulation properties and proteolysis of milk. Journal of Dairy Science, 103(5), 4043–4055. https://doi.org/10.3168/jds.2019-17771
[18] Mohammadi, A., Ghorbani, M., Sadeghi Mahoonak, A.R., Jafari, S.M. 2022. Evaluation and comparison of functional properties of whey protein isolate-inulin mixtures and conjugates. Food Processing and Preservation Journal, 14 (2), 71-88.
[19] Holt, J. G., Krieg, N. R., Sneath, P. H. A., Staley, J. T., & Williams, S. T. (1994). Bergey’s manual of determinative bacteriology (9th ed.). Williams & Wilkins.
[20] Forbes, B. A., Sahm, D. F., & Weissfeld, A. S. (2007). Bailey & Scott’s diagnostic microbiology (12th ed.). Mosby Elsevier.
[21] Nomura, K., Onda, K., Murase, H., Hashiya, F., Ono, Y., Terai, G., Oka, N., Asai, K., Suzuki, D., Takahashi, N., Hiraoka, H., Inagaki, M., Kimura, Y., Shimizu, Y., Abe, N., & Abe, H. (2024). Development of PCR primers enabling the design of flexible sticky ends for efficient concatenation of long DNA fragments. RSC Chemical Biology, 5(4). https://doi.org/10.1039/d3cb00212h
[22] Basu, I., Gorai, B., Chandran, T., et al. (2022). Selection of start codon during mRNA scanning in eukaryotic translation initiation. Communications Biology, 5, 587. https://doi.org/10.1038/s42003-022-03534-2
[23] Campbell, M., Mahenthiralingam, E., & Speert, D. P. (2000). Evaluation of random amplified polymorphic DNA typing of Pseudomonas aeruginosa. Journal of Clinical Microbiology, 38(12), 4614–4615. https://doi.org/10.1128/JCM.38.12.4614-4615.2000
[24] Hematzadeh, A., & Haghkhah, M. (2021). Biotyping of isolates of Pseudomonas aeruginosa isolated from human infections by RAPD and ERIC-PCR. Heliyon, 7(9), e07967. https://doi.org/10.1016/j.heliyon.2021.e07967
[25] Abdel-Rhman, S. H., & Rizk, D. E. (2021). Comparative assessment of different PCR-based typing methods of Pseudomonas aeruginosa isolates. Infection and Drug Resistance, 14, 1019–1035. https://doi.org/10.2147/IDR.S298838
[26] Sharma, V., Firth, A. E., Antonov, I., Fayet, O., Atkins, J. F., Borodovsky, M., & Baranov, P. V. (2011). A pilot study of bacterial genes with disrupted ORFs reveals a surprising profusion of protein sequence recoding mediated by ribosomal frameshifting and transcriptional realignment. Molecular Biology and Evolution, 28(11), 3195–3211. https://doi.org/10.1093/molbev/msr155
[27] Gai, N., Uniacke-Lowe, T., O'Regan, J., Goulding, D. A., Affolter, M., Fuerer, C., & Kelly, A. L. (2025). Proteolytic pathways in bovine milk containing β-CN A1 or A2. International Dairy Journal, 164, 106200. https://doi.org/10.1016/j.idairyj.2025.106200
[28] Glück, C., Rentschler, E., Krewinkel, M., Merz, M., von Neubeck, M., Wenning, M., Scherer, S., Stoeckel, M., Hinrichs, J., Stressler, T., & Fischer, L. (2016). Thermostability of peptidases secreted by microorganisms associated with raw milk. International Dairy Journal, 56, 186–197. https://doi.org/10.1016/j.idairyj.2016.01.025