Biosynthesis of the acid protease produced by Lacticaseibacillus casei LBC 237 and Limosilactobacillus fermentum LBF 433 and their potential application in the bovine milk clotting
Open accessIntegrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The quality of milk-clotting enzymes and thus their milk-clotting activity, proteolytic activity, and MCA/PA ratio depends on the method for obtaining enzymes, including cultivation temperature, initial pH of medium, nitrogen and carbon sources, and NaCl concentration.
“The quality of MCE and thus its MCA, PA, and the ratio of MCA to PA, depends on the method for obtaining enzymes (i.e., cultivation temperature, initial pH of medium, nitrogen and carbon sources, and NaCl concentration).”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Lacticaseibacillus casei (LBC-P) and Limosilactobacillus fermentum (LBF-P) synthesized acid protease displaying peak relative activity at 60°C, with proteolytic activity values of 144.6 U/mL and 135.8 U/mL, respectively.
“The results presented by Artifon et al. (2023) showed that Lb. casei (LBC-P) and Limosilactobacillus fermentum (LBF-P) synthesized the enzyme (acid protease), displaying peak relative activity at 60°C, with values of 144.6 U/mL and 135.8 U/mL PA, respectively.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
The proteolytic activity levels of LBC-P and LBF-P enzymes remained stable across all tested temperatures (30°C to 75°C at 5°C intervals).
“However, the PA levels of these enzymes remained stable across all tested temperatures (temperatures ranging between 30°C and 75°C at 5°C intervals).”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Both LBC-P and LBF-P exhibit a broad operating temperature range, making them effective in various processes that require acid proteases.
“These results indicate that both LBC-P and LBF-P exhibit a broad operating temperature range, making them effective in various processes that require acid proteases.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
The optimal temperature of activity of commercial chymosin was 45°C (PA = 23.40 U/mL), which is relatively low compared with microbial-derived milk-clotting proteases.
“The optimal temperature of activity was 45°C (PA = 23.40U/mL), which is relatively low compared with microbial-derived MCP.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
The functional groups of LBC-P and LBF-P milk-clotting enzymes remained stable under the examined pH conditions.
“This study revealed that the functional groups of these 2 MCE remained stable under the examined conditions.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
No signs of enzyme denaturation were observed across the tested pH range.
“In addition, no signs of enzyme denaturation were observed across the tested pH range.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
The highest proteolytic activity levels recorded were 81.4 U/mL for LBC-P, 95.1 U/mL for LBF-P, and 25.2 U/mL for chymosin.
“The highest PA levels recorded were 81.4 U/mL for LBC-P, 95.1 U/mL for LBF-P, and 25.2 U/mL for chymosin.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
All enzymes exhibit similar proteolytic activity values, regardless of the pH values used.
“Artifon et al. (2023) showed that all enzymes exhibit similar PA values, regardless of the pH values used.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Excessively high NaCl concentrations may cause enzyme denaturation, resulting in loss of activity.
“Sodium chloride improves the stability of casein micelles; however, excessively high concentrations may cause enzyme denaturation, resulting in loss of activity (Afsharnezhad et al., 2019;Artifon et al., 2023).”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Sodium chloride improves the stability of casein micelles.
“Sodium chloride improves the stability of casein micelles; however, excessively high concentrations may cause enzyme denaturation, resulting in loss of activity (Afsharnezhad et al., 2019;Artifon et al., 2023).”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
MCE from B. subtilis remained fully active within the NaCl range of 0.1% to 1%.
“In contrast, the MCE from B. subtilis remained fully active within the NaCl range of 0.1% to 1% (Artifon et al., 2023).”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Milk curd made using MCE from LBC was more porous than the milk curd obtained with chymosin.
“The milk curd made using MCE from LBC was more porous than the milk curd obtained with chymosin.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Decreased protein degradation can contribute to the formation of a more compact cheese structure.
“Artifon et al. (2023) stated that decreased protein degradation can contribute to the formation of a more compact cheese structure.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
An excessive degree of protein hydrolysis can cause increased water-soluble degradation products that negatively affect the formation of the protein matrix.
“Conversely, an excessive degree of protein hydrolysis can cause increased watersoluble degradation products that negatively affect the formation of the protein matrix (Artifon et al., 2023)”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Protease from Lb. casei (LBC 237) was able to break down casein bond types similar to those broken down by chymosin.
“Artifon et al. (2023) showed that protease from Lb. casei (LBC 237) was able to break down casein bond types similar to those that break down by chymosin.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Curd formation using LBC-P enzyme was inhibited at NaCl concentrations exceeding 1%.
“The impact of varying NaCl concentrations on milk coagulation using LBC-P enzyme was examined, revealing that curd formation was inhibited at concentrations exceeding 1%.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Hydrophobic peptides β-CN (f190-209) and β-CN (f193-209), typically associated with cheese bitterness, were produced in relatively low amounts in LBC-P curd.
“Artifon et al. (2023) showed that milk curd obtained with Lb. casei (LBC-P) exhibited lower bitterness than curd formed with chymosin, suggesting that the cor-responding hydrophobic peptides, β-CN (f190-209) and β-CN (f193-209), which are typically associated with cheese bitterness, were produced in relatively low amounts (Artifon et al., 2023;Li et al., 2022).”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Milk curd obtained with Lb. casei (LBC-P) exhibited lower bitterness than curd formed with chymosin.
“Artifon et al. (2023) showed that milk curd obtained with Lb. casei (LBC-P) exhibited lower bitterness than curd formed with chymosin, suggesting that the cor-responding hydrophobic peptides, β-CN (f190-209) and β-CN (f193-209), which are typically associated with cheese bitterness, were produced in relatively low amounts (Artifon et al., 2023;Li et al., 2022).”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
The addition of a greater quantity of alternative MCE can lead to pronounced bitterness.
“The addition of a greater quantity of alternative MCE can lead to pronounced bitterness.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Coagulants with a high MCA/PA ratio are preferred for cheese production because they help prevent excessive proteolysis, which can negatively affect cheese yield, texture, and flavor.
“Coagulants with a high MCA/PA ratio are preferred for cheese production because they help prevent excessive proteolysis, which can negatively affect cheese yield, texture, and flavor (Wehaidy et al., 2020;Artifon et al., 2023;Niero et al., 2024).”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Inadequate addition of MCE results in a weak cheese structure and a reduced cheese yield.
“Inadequate addition of MCE results in a weak cheese structure and a reduced cheese yield.”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Artifon et al., 2023
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Molecular and Biotechnological Aspects of Microbial Proteases
Rao, M. B., Tanksale, A. M., Ghatge, M. S., & DESHPANDE, V. V. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.3.597-635.1998 · Cited by 2,274 · see citing works
A COLORIMETRIC METHOD FOR THE DETERMINATION OF THE PROTEOLYTIC ACTIVITY OF DUODENAL JUICE
Charney, J., & Tomarelli, R. M. (1947) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41059-3 · Cited by 723 · see citing works
Microbial alkaline proteases: Optimization of production parameters and their properties
Sharma, K. M., Kumar, R., Panwar, S., & Kumar, A. (2017) · Journal of Genetic Engineering and Biotechnology · doi:10.1016/j.jgeb.2017.02.001 · Cited by 324 · see citing works
Recent Advances in Milk Clotting Enzymes
JACOB, M., JAROS, D., & ROHM, H. (2011) · International Journal of Dairy Technology · doi:10.1111/j.1471-0307.2010.00633.x · Cited by 295 · see citing works
Meng, Y., & Li, C. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.129622 · Cited by 281 · see citing works
Jurado, E., Camacho, F., Luzón, G., & Vicaria, J. M. (2003) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2003.07.004 · Cited by 128 · see citing works
Comparison of the Milk-Clotting Properties of Three Plant Extracts
Mazorra-Manzano, M. A., Perea-Gutiérrez, T. C., Lugo-Sánchez, M. E., Ramirez-Suarez, J. C., Torres-Llanez, M. J., González-Córdova, A. F., & Vallejo-Cordoba, B. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.05.042 · Cited by 117 · see citing works
Kinetic and thermodynamic studies of a novel acid protease from Aspergillus foetidus
Souza, P. M., Aliakbarian, B., Filho, E. X. F., Magalhães, P. O., Pessoa, A., Converti, A., & Perego, P. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.07.043 · Cited by 110 · see citing works
Kempka, A. P., Lipke, N., Pinheiro, T. D. L. F., Menoncin, S., Treichel, H., Freire, D. M. G., Luccio, M. D., & de Olíveira, D. (2007) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-007-0154-8 · Cited by 110 · see citing works
Self-citationA novel milk-clotting cysteine protease from Ficus johannis: Purification and characterization
Afsharnezhad, M., Shahangian, S. S., & Sariri, R. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.10.006 · Cited by 72 · see citing works
Ullah, N., Rehman, M. U., Sarwar, A., Nadeem, M., Nelofer, R., Shakir, H. A., Irfan, M. I., Idrees, M., Naz, S., Nabi, G., et al. (2022) · Fermentation · doi:10.3390/fermentation8110628 · Cited by 71 · see citing works
FTIR Imaging of Tissues: Techniques and Methods of Analysis
Małek, K., Wood, B. R., & Bambery, K. R. (2013) · Challenges and advances in computational chemistry and physics · doi:10.1007/978-94-007-7832-0_15 · Cited by 66 · see citing works
Anusha, R., Singh, M. K., & Bindhu, O. S. (2014) · European Food Research and Technology · doi:10.1007/s00217-014-2177-0 · Cited by 63 · see citing works
Majumder, R., Banik, S. P., & Khowala, S. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2014.10.027 · Cited by 59 · see citing works
de Castro, R. J. S., & Sato, H. H. (2013) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2013.12.002 · Cited by 56 · see citing works
Novel milk-clotting enzyme from Bacillus stearothermophilus as a coagulant in UF-white soft cheese
Ahmed, S. A., Wehaidy, H. R., Ibrahim, O. A., Abd El Ghani, S., & El-Hofi, M. A. (2016) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2016.06.011 · Cited by 45 · see citing works
Rennets: General and Molecular Aspects
Crabbe, M. (2004) · Cheese · doi:10.1016/s1874-558x(04)80061-7 · Cited by 42 · see citing works
Soltani, M., Boran, O. S., & Hayaloğlu, A. A. (2016) · LWT · doi:10.1016/j.lwt.2016.01.028 · Cited by 41 · see citing works
Xu, Y., Zhang, D., Chen, R., Yang, X., Liu, H., Wang, Z., & Hui, T. (2021) · Foods · doi:10.3390/foods10112676 · Cited by 38 · see citing works
Meng, F., Chen, R., Zhu, X., Lu, Y., Nie, T., Lu, F., & Lu, Z. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b01697 · Cited by 36 · see citing works
Zhao, X., Zheng, Z., Zhang, J., Sarwar, A., Aziz, T., & Yang, Z. (2019) · Food Science & Nutrition · doi:10.1002/fsn3.1003 · Cited by 29 · see citing works
Codon optimization of the calf prochymosin gene and its expression in Kluyveromyces lactis
Zhen, F., Zhang, L., Han, X., & Zhang, Y. (2009) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-009-0249-2 · Cited by 28 · see citing works
Hang, F., Wang, Q., Hong, Q., Liu, P., Wu, Z., Liu, Z., Zhang, H., & Chen, W. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.01.028 · Cited by 27 · see citing works
Gonçalves, M. C. P., Morales, S. A. V., da Silva, E. S., Maiorano, A. E., Perna, R. F., & Kieckbusch, T. G. (2020) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.6429 · Cited by 27 · see citing works
Silva, M. Z. R., de Oliveira, J. P. B., Ramos, M. V., Farias, D. F., de Sá, C. A., Ribeiro, J. A. C., Silva, A. F. B., de Sousa, J. S., Zambelli, R. A., da Silva, A. C., et al. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.125574 · Cited by 25 · see citing works
Abdel–Naby, M. A., El-Wafa, W. M. A., & Salem, G. E. M. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.05.241 · Cited by 25 · see citing works
Zhao, X., Cai, M., Yang, Z.-J., Luo, T.-Q., Sarwar, A., Megrous, S., Aziz, T., & Yang, Z.-N. (2019) · European Food Research and Technology · doi:10.1007/s00217-019-03361-6 · Cited by 24 · see citing works
Koka, R., & Weimer, B. C. (2000) · International Dairy Journal · doi:10.1016/s0958-6946(00)00023-6 · Cited by 22 · see citing works
Tarhan, Ö., & Kaya, A. (2021) · LWT · doi:10.1016/j.lwt.2021.112102 · Cited by 22 · see citing works
Purification and characteristics of a new milk-clotting enzyme from Bacillus licheniformis BL312
Zhang, Y., Xia, Y., Ding, Z., H. Lai, P. F., Wang, G., Xiong, Z., Liu, X., & Ai, L. (2019) · LWT · doi:10.1016/j.lwt.2019.108276 · Cited by 21 · see citing works
Wehaidy, H. R., Abdel Wahab, W. A., Kholif, A. M. M., Elaaser, M., Bahgaat, W. K., & Abdel-Naby, M. A. (2020) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2020.101589 · Cited by 21 · see citing works
Zaman, U., Khan, S. U., Alem, S. F. M., Rehman, K. U., Almehizia, A. A., Naglah, A. M., Al‐Wasidi, A. S., Refat, M. S. E.-D., Saeed, S., & Zaki, M. E. A. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.123217 · Cited by 21 · see citing works
Properties of a Milk-Clotting Microbial Enzyme
Melachouris, N., & Tuckey, S. L. (1968) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(68)87049-3 · Cited by 20 · see citing works
Tito, F. R., Pepe, A., Tonón, C. V., Daleo, G. R., & Guevara, M. G. (2020) · International Dairy Journal · doi:10.1016/j.idairyj.2020.104645 · Cited by 20 · see citing works
Şahingil, D., Gokce, Y., Çelikbıçak, Ö., & Hayaloğlu, A. A. (2022) · Journal of Food Composition and Analysis · doi:10.1016/j.jfca.2022.104579 · Cited by 20 · see citing works
Li, B., Waldron, D. S., Drake, M. A., Lyne, J., Kelly, A. L., & McSweeney, P. L. H. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2022.105346 · Cited by 19 · see citing works
Bouazizi, A., Felfoul, I., Attia, H., & Karoui, R. (2021) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2021.112312 · Cited by 18 · see citing works
Levels of antioxidant enzymes and alkaline protease from pulp and peel of sunflower
Mehdi, W. A., Yusof, F., Farhan, L. O., Mehde, A. A., & Raus, R. A. (2017) · Asian Pacific Journal of Tropical Biomedicine · doi:10.1016/j.apjtb.2017.05.002 · Cited by 17 · see citing works
Liu, L., Zhe, Z., Zhao, X. Y., Fengyu, W., Zhang, J., & Yang, Z. (2019) · Food Science and Biotechnology · doi:10.1007/s10068-018-0539-2 · Cited by 16 · see citing works
Li, G. Y., Cai, Y., Liao, X., & Yin, J. (2010) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-010-0855-x · Cited by 16 · see citing works
Baptista, D. P., & Gigante, M. L. (2022) · Applied Food Research · doi:10.1016/j.afres.2022.100107 · Cited by 13 · see citing works
El-Tanboly, E.-S., El-Hofi, M. A., Youssef, Y. B., El-Desoki, W., & ISMAIL, A. A. (2012) · Journal of Food and Dairy Sciences · doi:10.21608/jfds.2012.75391 · Cited by 13 · see citing works
Putranto, W. S., Suhartono, M. T., Kusumaningrum, H. D., Giriwono, P. E., & Mustopa, A. Z. (2020) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2020.101818 · Cited by 12 · see citing works
El-Tanboly, E.-S., El-Hofi, M. A., Youssef, Y. B., El-Desoki, W., & ISMAIL, A. A. (2013) · PubMed · Cited by 12 · see citing works
Leite, B. R. D. C., Tribst, A. A. L., & Cristianini, M. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.07.035 · Cited by 11 · see citing works
Wehaidy, H. R., Abdel–Naby, M. A., Kholif, A. M. M., Elaaser, M. M., Bahgaat, W. K., & Wahab, W. A. A. (2023) · Journal of Genetic Engineering and Biotechnology · doi:10.1186/s43141-023-00513-w · Cited by 10 · see citing works
An investigation of the enzymatic cleavage of κ-casein in non-coagulating milk
Nilsson, K., Abdelghani, A., Burleigh, S., Johansen, L. B., Lindmark-Månsson, H., Paulsson, M. A., & Glantz, M. (2020) · International Dairy Journal · doi:10.1016/j.idairyj.2020.104754 · Cited by 10 · see citing works
EFFECT OF COMMERCIAL PROTEASE ENZYME ON PROTEOLYSIS OF IRANIAN UF-FETA CHEESE
Akhgar, R. N. R., Hesari, J., & Azadmard‐Damirchi, S. (2017) · Cited by 3 · see citing works
Flagged first, then by citations
1 of the 50 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Wu, H., Zhang, H., Yan, R., Li, S., Guo, X., Qiu, L., & Yao, Y. (2024) · Advanced Science · doi:10.1002/advs.202406119 · Cited by 26 · see citing works
Bellaver, E. H., Redin, E. E., da Costa, I. M., Moroni, L. S., & Kempka, A. P. (2024) · Food Research International · doi:10.1016/j.foodres.2024.114060 · Cited by 23 · see citing works
Self-citationKautzmann, C., CASTANHA, E., Dammann, C. A. J., de Jesus, B. A. P., da Silva, G. F., Magalhães, M. D. L. B., Deolindo, C. T. P., & Kempka, A. P. (2024) · Food Research International · doi:10.1016/j.foodres.2024.114206 · Cited by 23 · see citing works
Self-citationBioactive whey peptides: a bibliometric and functional overview
Sumny, E. H., & Kempka, A. P. (2025) · Discover Food · doi:10.1007/s44187-025-00430-6 · Cited by 13 · see citing works
Self-citationBellaver, E. H., da Costa, I. M., Redin, E. E., Moroni, L. S., & Kempka, A. P. (2024) · Intelligent Pharmacy · doi:10.1016/j.ipha.2024.05.009 · Cited by 12 · see citing works
Self-citationInvited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review.
Wiśniewski, P., Małkowska-Kowalczyk, M., Łobacz, A., Zadernowska, A., & Żulewska, J. (2025) · Journal of dairy science · doi:10.3168/jds.2025-26973 · Cited by 10 · see citing works
Bellaver, E. H., da Costa, I. M., Redin, E. E., Moroni, L. S., Cunico, L. P., Bourckhardt, L. E. H., Cécere, B. G. D. O., da Silva, A. S., & Kempka, A. P. (2025) · International Dairy Journal · doi:10.1016/j.idairyj.2025.106450 · Cited by 4 · see citing works
Self-citationWei, G., Wang, T., Wang, Y. Y., Zhang, W., Li, Y., Chai, Y., Wang, X. Q., & Huang, A. (2026) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.70392 · Cited by 4 · see citing works
Extraction, catalytic study and milk-clotting properties of proteases from Brassica oleracea
Fabrizi, C., Liburdi, K., & Esti, M. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.104396 · Cited by 3 · see citing works
Bellaver, E. H., Redin, E. E., da Costa, I. M., Moroni, L. S., & Kempka, A. P. (2025) · ACS Food Science & Technology · doi:10.1021/acsfoodscitech.5c00396 · Cited by 1 · see citing works
Self-citationPutri, A. A., Rustama, M. M., & Putranto, W. S. (2023) · Jurnal Teknologi Hasil Peternakan · doi:10.24198/jthp.v4i2.49924
da Silva, E. C., Santos, M. P. F., Teixeira, J. M., Costa, F. S., Fontan, R. D. C. I., Veloso, C. M., Franco, M., & Bonomo, R. C. F. (2026) · Bioresource Technology Reports · doi:10.1016/j.biteb.2026.102663
Brunetto, A. L. R., Nora, L., Giacomelli, C. M., Deolindo, G. L., Silva, L. E. L. E., Wagner, R. C., Kozloski, G. V., & da Silva, A. S. (2026) · Ruminants · doi:10.3390/ruminants6020043
Ai, C., Hu, Y., Wang, L. T., Ren, X., & Song, S. (2026) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2026.111918
Madler, A. K., Kennedy, K., Morel, E. F., Brock, A., Alcaine, S. D., & Lei, X. G. (2026) · Journal of Dairy Science · doi:10.3168/jds.2026-28550
- Authors
- Artifon, S. E. S., Sumny, E. H., Fabris, T., de Jesus, B. A. P., Magalhães, M. D. L. B., Silva, G. F. D., Dognini, J., Andrade, N. C., Moroni, L. S., & Kempka, A. P.
- Affiliations
- Universidade do Estado de Santa Catarina (BR)
- Serviço Nacional de Aprendizagem Industrial (BR)
- Corresponding author
- Kempka, Aniela Pinto
- ORCID
- Venue
- Food Bioscience
- Publisher
- Elsevier BV
- Published
- 2023-08
- Volume
- 54
- Pages
- 102879
- ISSN
- 2212-4292 (ISSN-L)
- OpenAlex
- W4381331641
- Cited by
- 15
- References
- 50
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 5 · 2023: 1
- FWCI
- 1.94
- Type
- journal article
- Language
- en
- Open access
- green
- repositorio.udesc.br
- Licence
- Locations
- Food Bioscience (publishedVersion)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (submittedVersion, other-oa)
- Funders
- Conselho Nacional de Desenvolvimento Científico e Tecnológico (303915/2022-6)
- Fundação de Amparo à Pesquisa e Inovação do Estado de Santa Catarina (2021TR1757, 2021TR797)
- Universidade do Estado de Santa Catarina
- Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Keywords
- aspartic protease, Lactobacillus casei, Lactobacillus fermentum, milk coagulation, cheese starter cultures, protease stability, proteolytic activity, cheese bitterness, cheese flavor, cheese texture
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
