Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics
Само за регистроване кориснике
2016
Аутори
Jovanović, JelenaStefanović, Andrea
Šekuljica, Nataša
Jakovetić Tanasković, Sonja
Dojčinović, Marina
Bugarski, Branko
Knežević-Jugović, Zorica
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
The impact of ultrasound waves generated by probe-type sonicator and ultrasound cleaning bath on egg white protein susceptibility to hydrolysis by alcalase compared to both thermal pretreatment and conventional enzymatic hydrolysis was quantitatively investigated. A series of hydrolytic reactions was carried out in a stirred tank reactor at different substrate concentrations, enzyme concentrations, and temperatures using untreated, and pretreated egg white proteins (EWPs). The kinetic model based on substrate inhibition and second-order enzyme deactivation successfully predicts the experimental behavior providing an effective tool for comparison and optimization. The ultrasound pretreatments appear to greatly improve the enzymatic hydrolysis of EWPs under different conditions when compare to other methods. The apparent reaction rate constants for proteolysis (k(2)) are 0.009, 0.011, 0.053, and 0.045 min(-1) for untreated EWPs, and those pretreated with heat, probe-type sonicator, and u...ltrasound cleaning bath technologies, respectively. The ultrasound pretreatment also decreases hydrolysis activation (E-a) and enzyme deactivation (E-d) energy, enthalpy (Delta H), and entropy (Delta S) of activation and for the probe-type sonication this decrease is 61.7%, 61.6%, 63.6%, and 32.2%, respectively, but ultrasound has little change in Gibbs free energy value in the temperature range of 318 to 338 K. The content of sulfhydryl groups and zeta potential show a significant increase (P lt 0.05) for both applied ultrasound pretreatments and the reduction of particle size distribution are achieved, providing some evidence that the ultrasound causes EWP structural changes affecting the proteolysis rate.
Кључне речи:
enzymatic hydrolysis / EWPs / kinetic model / particle characteristics / ultrasound pretreatmentИзвор:
Journal of Food Science, 2016, 81, 11, C2664-C2675Издавач:
- Wiley, Hoboken
Финансирање / пројекти:
- E!6750
- Развој нових инкапсулационих и ензимских технологија за производњу биокатализатора и биолошки активних компонената хране у циљу повећања њене конкурентности, квалитета и безбедности (RS-MESTD-Integrated and Interdisciplinary Research (IIR or III)-46010)
DOI: 10.1111/1750-3841.13503
ISSN: 0022-1147
PubMed: 27680882
WoS: 000388953400014
Scopus: 2-s2.0-84989361009
Колекције
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Jovanović, Jelena AU - Stefanović, Andrea AU - Šekuljica, Nataša AU - Jakovetić Tanasković, Sonja AU - Dojčinović, Marina AU - Bugarski, Branko AU - Knežević-Jugović, Zorica PY - 2016 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/3309 AB - The impact of ultrasound waves generated by probe-type sonicator and ultrasound cleaning bath on egg white protein susceptibility to hydrolysis by alcalase compared to both thermal pretreatment and conventional enzymatic hydrolysis was quantitatively investigated. A series of hydrolytic reactions was carried out in a stirred tank reactor at different substrate concentrations, enzyme concentrations, and temperatures using untreated, and pretreated egg white proteins (EWPs). The kinetic model based on substrate inhibition and second-order enzyme deactivation successfully predicts the experimental behavior providing an effective tool for comparison and optimization. The ultrasound pretreatments appear to greatly improve the enzymatic hydrolysis of EWPs under different conditions when compare to other methods. The apparent reaction rate constants for proteolysis (k(2)) are 0.009, 0.011, 0.053, and 0.045 min(-1) for untreated EWPs, and those pretreated with heat, probe-type sonicator, and ultrasound cleaning bath technologies, respectively. The ultrasound pretreatment also decreases hydrolysis activation (E-a) and enzyme deactivation (E-d) energy, enthalpy (Delta H), and entropy (Delta S) of activation and for the probe-type sonication this decrease is 61.7%, 61.6%, 63.6%, and 32.2%, respectively, but ultrasound has little change in Gibbs free energy value in the temperature range of 318 to 338 K. The content of sulfhydryl groups and zeta potential show a significant increase (P lt 0.05) for both applied ultrasound pretreatments and the reduction of particle size distribution are achieved, providing some evidence that the ultrasound causes EWP structural changes affecting the proteolysis rate. PB - Wiley, Hoboken T2 - Journal of Food Science T1 - Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics EP - C2675 IS - 11 SP - C2664 VL - 81 DO - 10.1111/1750-3841.13503 ER -
@article{ author = "Jovanović, Jelena and Stefanović, Andrea and Šekuljica, Nataša and Jakovetić Tanasković, Sonja and Dojčinović, Marina and Bugarski, Branko and Knežević-Jugović, Zorica", year = "2016", abstract = "The impact of ultrasound waves generated by probe-type sonicator and ultrasound cleaning bath on egg white protein susceptibility to hydrolysis by alcalase compared to both thermal pretreatment and conventional enzymatic hydrolysis was quantitatively investigated. A series of hydrolytic reactions was carried out in a stirred tank reactor at different substrate concentrations, enzyme concentrations, and temperatures using untreated, and pretreated egg white proteins (EWPs). The kinetic model based on substrate inhibition and second-order enzyme deactivation successfully predicts the experimental behavior providing an effective tool for comparison and optimization. The ultrasound pretreatments appear to greatly improve the enzymatic hydrolysis of EWPs under different conditions when compare to other methods. The apparent reaction rate constants for proteolysis (k(2)) are 0.009, 0.011, 0.053, and 0.045 min(-1) for untreated EWPs, and those pretreated with heat, probe-type sonicator, and ultrasound cleaning bath technologies, respectively. The ultrasound pretreatment also decreases hydrolysis activation (E-a) and enzyme deactivation (E-d) energy, enthalpy (Delta H), and entropy (Delta S) of activation and for the probe-type sonication this decrease is 61.7%, 61.6%, 63.6%, and 32.2%, respectively, but ultrasound has little change in Gibbs free energy value in the temperature range of 318 to 338 K. The content of sulfhydryl groups and zeta potential show a significant increase (P lt 0.05) for both applied ultrasound pretreatments and the reduction of particle size distribution are achieved, providing some evidence that the ultrasound causes EWP structural changes affecting the proteolysis rate.", publisher = "Wiley, Hoboken", journal = "Journal of Food Science", title = "Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics", pages = "C2675-C2664", number = "11", volume = "81", doi = "10.1111/1750-3841.13503" }
Jovanović, J., Stefanović, A., Šekuljica, N., Jakovetić Tanasković, S., Dojčinović, M., Bugarski, B.,& Knežević-Jugović, Z.. (2016). Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics. in Journal of Food Science Wiley, Hoboken., 81(11), C2664-C2675. https://doi.org/10.1111/1750-3841.13503
Jovanović J, Stefanović A, Šekuljica N, Jakovetić Tanasković S, Dojčinović M, Bugarski B, Knežević-Jugović Z. Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics. in Journal of Food Science. 2016;81(11):C2664-C2675. doi:10.1111/1750-3841.13503 .
Jovanović, Jelena, Stefanović, Andrea, Šekuljica, Nataša, Jakovetić Tanasković, Sonja, Dojčinović, Marina, Bugarski, Branko, Knežević-Jugović, Zorica, "Ultrasound Pretreatment as an Useful Tool to Enhance Egg White Protein Hydrolysis: Kinetics, Reaction Model, and Thermodinamics" in Journal of Food Science, 81, no. 11 (2016):C2664-C2675, https://doi.org/10.1111/1750-3841.13503 . .