TY  - JOUR
AU  - Vrhovac, Lidija
AU  - Šelemetjev, Sonja A.
AU  - Vatić, Saša
AU  - Mitrović, Aleksandar
AU  - Milošević, Jelica
AU  - Lolić, Aleksandar
AU  - Beletić, Anđelo D.
AU  - Polović, Natalija
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4295
AB  - Measurement of antithyroglobulin antibodies (TgAb) is an inevitable laboratory tool in the management of thyroid gland diseases. Currently available immunoassays still have limitations underlying the necessity of the introduction of fast, sensitive, and label-free technologies. Our aim was to develop a method for TgAb measurement in human serum based on the quartz crystal microbalance (QCM) technology. We immobilized thyroglobulin on the surface of Attana LNB Carboxyl sensor chip®, prepared standard curve covering the range of 1–50000 kIU/L, and established optimal measurement conditions. The validation included determination of the detection limit (LOD), functional sensitivity, linearity, precision, as well as the comparison with the results of the radioimmunoassay (RIA). The LOD and functional sensitivity were 4.2 kIU/L and 4.7 kIU/L, respectively. The method was linear in the range of 20–10000 kIU/L. The regression equation for comparison with RIA was CQCM = 1.0056 • CRIA – 24.2778, whereby no significant proportional or systematic difference was present. There was a good agreement with RIA in the classification of patients according to the clinical significance of the results. The developed method has advantages over currently available assays in terms of better LOQ, a higher upper limit of linearity, and precision. The characteristics of the developed method unambiguously show that the application of the QCM biosensors offers a highly reliable novel approach for the measurement of TgAb in human serum.
PB  - Elsevier
T2  - Talanta
T1  - Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors
VL  - 223
SP  - 121588
DO  - 10.1016/j.talanta.2020.121588
ER  - 

@article{
author = "Vrhovac, Lidija and Šelemetjev, Sonja A. and Vatić, Saša and Mitrović, Aleksandar and Milošević, Jelica and Lolić, Aleksandar and Beletić, Anđelo D. and Polović, Natalija",
year = "2021",
abstract = "Measurement of antithyroglobulin antibodies (TgAb) is an inevitable laboratory tool in the management of thyroid gland diseases. Currently available immunoassays still have limitations underlying the necessity of the introduction of fast, sensitive, and label-free technologies. Our aim was to develop a method for TgAb measurement in human serum based on the quartz crystal microbalance (QCM) technology. We immobilized thyroglobulin on the surface of Attana LNB Carboxyl sensor chip®, prepared standard curve covering the range of 1–50000 kIU/L, and established optimal measurement conditions. The validation included determination of the detection limit (LOD), functional sensitivity, linearity, precision, as well as the comparison with the results of the radioimmunoassay (RIA). The LOD and functional sensitivity were 4.2 kIU/L and 4.7 kIU/L, respectively. The method was linear in the range of 20–10000 kIU/L. The regression equation for comparison with RIA was CQCM = 1.0056 • CRIA – 24.2778, whereby no significant proportional or systematic difference was present. There was a good agreement with RIA in the classification of patients according to the clinical significance of the results. The developed method has advantages over currently available assays in terms of better LOQ, a higher upper limit of linearity, and precision. The characteristics of the developed method unambiguously show that the application of the QCM biosensors offers a highly reliable novel approach for the measurement of TgAb in human serum.",
publisher = "Elsevier",
journal = "Talanta",
title = "Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors",
volume = "223",
pages = "121588",
doi = "10.1016/j.talanta.2020.121588"
}

Vrhovac, L., Šelemetjev, S. A., Vatić, S., Mitrović, A., Milošević, J., Lolić, A., Beletić, A. D.,& Polović, N.. (2021). Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors. in Talanta
Elsevier., 223, 121588.
https://doi.org/10.1016/j.talanta.2020.121588

Vrhovac L, Šelemetjev SA, Vatić S, Mitrović A, Milošević J, Lolić A, Beletić AD, Polović N. Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors. in Talanta. 2021;223:121588.
doi:10.1016/j.talanta.2020.121588 .

Vrhovac, Lidija, Šelemetjev, Sonja A., Vatić, Saša, Mitrović, Aleksandar, Milošević, Jelica, Lolić, Aleksandar, Beletić, Anđelo D., Polović, Natalija, "Novel approach to the measurement of antithyroglobulin antibodies in human serum – application of the quartz crystal microbalance sensors" in Talanta, 223 (2021):121588,
https://doi.org/10.1016/j.talanta.2020.121588 . .

TY  - JOUR
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S1389172320303996
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4779
AB  - Trypsin is a serine protease with important applications such as protein sequencing and tissue dissociation. Preserving protein structure and its activity during freeze-thawing and prolonging its shelf life is one of the most interesting tasks in biochemistry. In the present study, trypsin cryoprotection was achieved by altering buffer composition. Sodium phosphate buffer at pH 8.0 led to pH shift-induced destabilization of trypsin and formation of a molten globule, followed by significant activity loss (about 70%). Potassium phosphate and ammonium bicarbonate buffers at pH 8.0 were used with up to 90% activity recovery rate after 7 freeze-thaw cycles. The addition of non-ionic surfactants Tween 20 and Tween 80 led to up to 99% activity recovery rate. Amide I region changes, corresponding to specific secondary structures in the Fourier transform infrared (FTIR) spectrum, were modest in the case of Tween 20 and Tween 80. On the other hand, the addition of Triton X-100 led to the destabilization of α-helicoidal segments of trypsin structure after 7 freeze-thaw cycles but also increased protein substrate availability.
PB  - Elsevier
T2  - Journal of Bioscience and Bioengineering
T1  - Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants
VL  - 131
IS  - 3
SP  - 234
EP  - 240
DO  - 10.1016/j.jbiosc.2020.10.010
ER  - 

@article{
author = "Vatić, Saša and Mirković, Nemanja and Milošević, Jelica and Jovčić, Branko and Polović, Natalija",
year = "2021",
abstract = "Trypsin is a serine protease with important applications such as protein sequencing and tissue dissociation. Preserving protein structure and its activity during freeze-thawing and prolonging its shelf life is one of the most interesting tasks in biochemistry. In the present study, trypsin cryoprotection was achieved by altering buffer composition. Sodium phosphate buffer at pH 8.0 led to pH shift-induced destabilization of trypsin and formation of a molten globule, followed by significant activity loss (about 70%). Potassium phosphate and ammonium bicarbonate buffers at pH 8.0 were used with up to 90% activity recovery rate after 7 freeze-thaw cycles. The addition of non-ionic surfactants Tween 20 and Tween 80 led to up to 99% activity recovery rate. Amide I region changes, corresponding to specific secondary structures in the Fourier transform infrared (FTIR) spectrum, were modest in the case of Tween 20 and Tween 80. On the other hand, the addition of Triton X-100 led to the destabilization of α-helicoidal segments of trypsin structure after 7 freeze-thaw cycles but also increased protein substrate availability.",
publisher = "Elsevier",
journal = "Journal of Bioscience and Bioengineering",
title = "Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants",
volume = "131",
number = "3",
pages = "234-240",
doi = "10.1016/j.jbiosc.2020.10.010"
}

Vatić, S., Mirković, N., Milošević, J., Jovčić, B.,& Polović, N.. (2021). Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants. in Journal of Bioscience and Bioengineering
Elsevier., 131(3), 234-240.
https://doi.org/10.1016/j.jbiosc.2020.10.010

Vatić S, Mirković N, Milošević J, Jovčić B, Polović N. Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants. in Journal of Bioscience and Bioengineering. 2021;131(3):234-240.
doi:10.1016/j.jbiosc.2020.10.010 .

Vatić, Saša, Mirković, Nemanja, Milošević, Jelica, Jovčić, Branko, Polović, Natalija, "Trypsin activity and freeze-thaw stability in the presence of ions and non-ionic surfactants" in Journal of Bioscience and Bioengineering, 131, no. 3 (2021):234-240,
https://doi.org/10.1016/j.jbiosc.2020.10.010 . .

TY  - JOUR
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4090
AB  - Numerous applications of proteolytic enzymes include dissociation of fermented meat products for the enumeration of `foodborne pathogenic bacteria. The use of trypsin for this cause is abandoned due to the high concentration of the enzyme affecting released bacteria. Papain, as a suggested replacement, and fig latex preparation with high extent of papain-like enzymes have the potential to be applied for bacteria enumeration. Both enzymatic preparations, originating from papaya and fig, showed a broader range of substrate specificities including gelatinolytic activity, especially prominent in the case of ficin and attributed to both, cysteine protease ficin and serine protease by the analysis of 2D zymography with specific inhibitors. The activity towards native collagen, mild in the case of papain, and extensive in the case of fig latex was proved by structural analysis of digested collagen by infrared spectroscopy. Further exploration of their potential for dissociation of fermented meat products showed that both papain and fig latex enzymes are stable in the presence of detergents Tween 20 and Triton X-100 and effective in the enumeration of Listeria monocytogenes. Gelatenolytic activity, and at least partial collagenolytic activity and stability in procedure conditions make papaya and fig latex proteases potent for this application in significantly lower concentrations than previously used enzymes. As a mixture of proteolytic enzymes with divergent characteristics, fig latex preparation shows higher efficiency in Listeria monocytogenes release than papain, conserved even in the presence of stronger non-ionic detergent Triton X-100.
PB  - Elsevier
T2  - International Journal of Food Microbiology
T1  - Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes
VL  - 334
SP  - 108851
DO  - 10.1016/j.ijfoodmicro.2020.108851
ER  - 

@article{
author = "Vatić, Saša and Mirković, Nemanja and Milošević, Jelica and Jovčić, Branko and Polović, Natalija",
year = "2020",
abstract = "Numerous applications of proteolytic enzymes include dissociation of fermented meat products for the enumeration of `foodborne pathogenic bacteria. The use of trypsin for this cause is abandoned due to the high concentration of the enzyme affecting released bacteria. Papain, as a suggested replacement, and fig latex preparation with high extent of papain-like enzymes have the potential to be applied for bacteria enumeration. Both enzymatic preparations, originating from papaya and fig, showed a broader range of substrate specificities including gelatinolytic activity, especially prominent in the case of ficin and attributed to both, cysteine protease ficin and serine protease by the analysis of 2D zymography with specific inhibitors. The activity towards native collagen, mild in the case of papain, and extensive in the case of fig latex was proved by structural analysis of digested collagen by infrared spectroscopy. Further exploration of their potential for dissociation of fermented meat products showed that both papain and fig latex enzymes are stable in the presence of detergents Tween 20 and Triton X-100 and effective in the enumeration of Listeria monocytogenes. Gelatenolytic activity, and at least partial collagenolytic activity and stability in procedure conditions make papaya and fig latex proteases potent for this application in significantly lower concentrations than previously used enzymes. As a mixture of proteolytic enzymes with divergent characteristics, fig latex preparation shows higher efficiency in Listeria monocytogenes release than papain, conserved even in the presence of stronger non-ionic detergent Triton X-100.",
publisher = "Elsevier",
journal = "International Journal of Food Microbiology",
title = "Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes",
volume = "334",
pages = "108851",
doi = "10.1016/j.ijfoodmicro.2020.108851"
}

Vatić, S., Mirković, N., Milošević, J., Jovčić, B.,& Polović, N.. (2020). Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes. in International Journal of Food Microbiology
Elsevier., 334, 108851.
https://doi.org/10.1016/j.ijfoodmicro.2020.108851

Vatić S, Mirković N, Milošević J, Jovčić B, Polović N. Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes. in International Journal of Food Microbiology. 2020;334:108851.
doi:10.1016/j.ijfoodmicro.2020.108851 .

Vatić, Saša, Mirković, Nemanja, Milošević, Jelica, Jovčić, Branko, Polović, Natalija, "Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes" in International Journal of Food Microbiology, 334 (2020):108851,
https://doi.org/10.1016/j.ijfoodmicro.2020.108851 . .

TY  - DATA
AU  - Vatić, Saša
AU  - Mirković, Nemanja
AU  - Milošević, Jelica
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4091
PB  - Elsevier
T2  - International Journal of Food Microbiology
T1  - Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4091
ER  - 

@misc{
author = "Vatić, Saša and Mirković, Nemanja and Milošević, Jelica and Jovčić, Branko and Polović, Natalija",
year = "2020",
publisher = "Elsevier",
journal = "International Journal of Food Microbiology",
title = "Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4091"
}

Vatić, S., Mirković, N., Milošević, J., Jovčić, B.,& Polović, N.. (2020). Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851. in International Journal of Food Microbiology
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4091

Vatić S, Mirković N, Milošević J, Jovčić B, Polović N. Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851. in International Journal of Food Microbiology. 2020;.
https://hdl.handle.net/21.15107/rcub_cherry_4091 .

Vatić, Saša, Mirković, Nemanja, Milošević, Jelica, Jovčić, Branko, Polović, Natalija, "Supplementary data for the article: Vatić, S.; Mirković, N.; Milošević, J. R.; Jovčić, B.; Polović, N. Đ. Broad Range of Substrate Specificities in Papain and Fig Latex Enzymes Preparations Improve Enumeration of Listeria Monocytogenes. International Journal of Food Microbiology 2020, 334, 108851. https://doi.org/10.1016/j.ijfoodmicro.2020.108851" in International Journal of Food Microbiology (2020),
https://hdl.handle.net/21.15107/rcub_cherry_4091 .

TY  - DATA
AU  - Rašković, Brankica
AU  - Vatić, Saša
AU  - Anđelković, Boban D.
AU  - Blagojević, Vladimir A.
AU  - Polović, Natalija
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3586
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochemical Engineering Journal
T1  - Supplementary material for the article: Rašković, B.; Vatić, S.; Andelković, B.; Blagojević, V.; Polović, N. Optimizing Storage  Conditions to Prevent Cold Denaturation of Trypsin for Sequencing and to Prolong Its Shelf  Life. Biochemical Engineering Journal 2016, 105, 168–176.  https://doi.org/10.1016/j.bej.2015.09.018
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3586
ER  - 

@misc{
author = "Rašković, Brankica and Vatić, Saša and Anđelković, Boban D. and Blagojević, Vladimir A. and Polović, Natalija",
year = "2016",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochemical Engineering Journal",
title = "Supplementary material for the article: Rašković, B.; Vatić, S.; Andelković, B.; Blagojević, V.; Polović, N. Optimizing Storage  Conditions to Prevent Cold Denaturation of Trypsin for Sequencing and to Prolong Its Shelf  Life. Biochemical Engineering Journal 2016, 105, 168–176.  https://doi.org/10.1016/j.bej.2015.09.018",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3586"
}

Rašković, B., Vatić, S., Anđelković, B. D., Blagojević, V. A.,& Polović, N.. (2016). Supplementary material for the article: Rašković, B.; Vatić, S.; Andelković, B.; Blagojević, V.; Polović, N. Optimizing Storage  Conditions to Prevent Cold Denaturation of Trypsin for Sequencing and to Prolong Its Shelf  Life. Biochemical Engineering Journal 2016, 105, 168–176.  https://doi.org/10.1016/j.bej.2015.09.018. in Biochemical Engineering Journal
Elsevier Science Bv, Amsterdam..
https://hdl.handle.net/21.15107/rcub_cherry_3586

Rašković B, Vatić S, Anđelković BD, Blagojević VA, Polović N. Supplementary material for the article: Rašković, B.; Vatić, S.; Andelković, B.; Blagojević, V.; Polović, N. Optimizing Storage  Conditions to Prevent Cold Denaturation of Trypsin for Sequencing and to Prolong Its Shelf  Life. Biochemical Engineering Journal 2016, 105, 168–176.  https://doi.org/10.1016/j.bej.2015.09.018. in Biochemical Engineering Journal. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3586 .

Rašković, Brankica, Vatić, Saša, Anđelković, Boban D., Blagojević, Vladimir A., Polović, Natalija, "Supplementary material for the article: Rašković, B.; Vatić, S.; Andelković, B.; Blagojević, V.; Polović, N. Optimizing Storage  Conditions to Prevent Cold Denaturation of Trypsin for Sequencing and to Prolong Its Shelf  Life. Biochemical Engineering Journal 2016, 105, 168–176.  https://doi.org/10.1016/j.bej.2015.09.018" in Biochemical Engineering Journal (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3586 .

TY  - JOUR
AU  - Rašković, Brankica
AU  - Vatić, Saša
AU  - Anđelković, Boban D.
AU  - Blagojević, Vladimir A.
AU  - Polović, Natalija
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2024
AB  - Trypsin is a serine protease with widespread applications, including protein sequencing and typsin mass fingerprinting. In the present study, the storage of trypsin in acidic conditions significantly affected the recovery of activity (40%) after 7 freeze-thaw cycles. Further, trypsin lost parts of its native secondary structure elements, which resulted in a 10% increase in beta-sheet content (band maximum detected at a frequency of 1634 cm in the Fourier transform infrared (FT-IR) spectrum) indicative of freezing-induced denaturation of the protein. The cold storage of trypsin in ammonium bicarbonate (pH 8.2) with the addition of ayoprotectants, such as glycerol or lysine, led to protein stabilization (complete secondary structure content preservation was detected by FT-IR), higher activity recovery ( gt 90%) and modest autolysis ( lt 10%). High activity recovery ( gt 90%) was also detected with the addition of propylene glycol and polyethylene glycol, saccharides and arginine. Nevertheless, trypsin stored at pH 8.2 with the addition of glycerol or lysine was as efficient as untreated trypsin in the trypsin mass fingerprinting analysis of BSA, suggesting that the cold storage of trypsin in slightly alkaline conditions with the addition of cryoprotectants could prolong its shelf life. (C) 2015 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochemical Engineering Journal
T1  - Optimizing storage conditions to prevent cold denaturation of trypsin for sequencing and to prolong its shelf life
VL  - 105
SP  - 168
EP  - 176
DO  - 10.1016/j.bej.2015.09.018
ER  - 

@article{
author = "Rašković, Brankica and Vatić, Saša and Anđelković, Boban D. and Blagojević, Vladimir A. and Polović, Natalija",
year = "2016",
abstract = "Trypsin is a serine protease with widespread applications, including protein sequencing and typsin mass fingerprinting. In the present study, the storage of trypsin in acidic conditions significantly affected the recovery of activity (40%) after 7 freeze-thaw cycles. Further, trypsin lost parts of its native secondary structure elements, which resulted in a 10% increase in beta-sheet content (band maximum detected at a frequency of 1634 cm in the Fourier transform infrared (FT-IR) spectrum) indicative of freezing-induced denaturation of the protein. The cold storage of trypsin in ammonium bicarbonate (pH 8.2) with the addition of ayoprotectants, such as glycerol or lysine, led to protein stabilization (complete secondary structure content preservation was detected by FT-IR), higher activity recovery ( gt 90%) and modest autolysis ( lt 10%). High activity recovery ( gt 90%) was also detected with the addition of propylene glycol and polyethylene glycol, saccharides and arginine. Nevertheless, trypsin stored at pH 8.2 with the addition of glycerol or lysine was as efficient as untreated trypsin in the trypsin mass fingerprinting analysis of BSA, suggesting that the cold storage of trypsin in slightly alkaline conditions with the addition of cryoprotectants could prolong its shelf life. (C) 2015 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochemical Engineering Journal",
title = "Optimizing storage conditions to prevent cold denaturation of trypsin for sequencing and to prolong its shelf life",
volume = "105",
pages = "168-176",
doi = "10.1016/j.bej.2015.09.018"
}

Rašković, B., Vatić, S., Anđelković, B. D., Blagojević, V. A.,& Polović, N.. (2016). Optimizing storage conditions to prevent cold denaturation of trypsin for sequencing and to prolong its shelf life. in Biochemical Engineering Journal
Elsevier Science Bv, Amsterdam., 105, 168-176.
https://doi.org/10.1016/j.bej.2015.09.018

Rašković B, Vatić S, Anđelković BD, Blagojević VA, Polović N. Optimizing storage conditions to prevent cold denaturation of trypsin for sequencing and to prolong its shelf life. in Biochemical Engineering Journal. 2016;105:168-176.
doi:10.1016/j.bej.2015.09.018 .

Rašković, Brankica, Vatić, Saša, Anđelković, Boban D., Blagojević, Vladimir A., Polović, Natalija, "Optimizing storage conditions to prevent cold denaturation of trypsin for sequencing and to prolong its shelf life" in Biochemical Engineering Journal, 105 (2016):168-176,
https://doi.org/10.1016/j.bej.2015.09.018 . .