The DOI matches its Crossref record.
High intensity ultrasound treatment of faba bean (Vicia faba L.) protein: Effect on surface properties, foaming ability and structural changes
Abstract
Response surface methodology was used for establishing the amplitude (72.67%) and time (17.29 min) high-intensity ultrasound (HIUS) conditions leading to an optimized faba bean protein isolate (OFPI) with lower interfacial tension, zeta potential and viscosity, and higher solubility than native faba bean protein isolate (NFPI). OFPI showed significantly higher adsorption dynamics at the air-water interface, and produced foam with significant smaller bubble diameter, higher overrun, stability and yield stress, and lower liquid drainage than NFPI. Fourier Transform Spectroscopy (FT-IR) revealed that the secondary structure of OFPI deferred from NFPI in terms of increases in β conformations (6.61% β-sheet, 19.6% β-turn, 0.8% anti-parallel β-sheet) and decreases in inter-molecular aggregates (43.54%). Multienzyme study pinpointed that the structural changes could have induced a decrease on the relative protein digestibility of OFPI respect that of NFPI. The results of this work demonstrate that HIUS technology improves the surface and foaming properties of faba bean protein isolate, which may favour the revalorisation of this crop.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 42
- Vioque, 2012, Nutritional and functional properties of Vicia faba protein isolates and related fractions, Food Chem., 132, 67, 10.1016/j.foodchem.2011.10.033 · DOI
- Pérez, 2014, Application of multivariate methods to identify outstanding broad bean cultivars for the State of Mexico, Rev. Mex. Cienc. Agric., 5, 265
- Parmar, 2017, Protein and microstructure evaluation of harder-to-cook and easy-to-cook grains from different kidney bean accessions, LWT – Food Sci. Technol., 79, 487, 10.1016/j.lwt.2017.01.027 · DOI
- Cepeda, 1998, Functional properties of faba bean (Vicia faba) protein flour dried by spray drying and freeze drying, J. Food Eng., 36, 303, 10.1016/S0260-8774(98)00061-2 · DOI
- Arogundade, 2006, Effect of ionic strength and/or pH on extractability and physico-functional characterization of broad bean (Vicia faba L.) protein concentrate, Food Hydrocoll., 20, 1124, 10.1016/j.foodhyd.2005.12.010 · DOI
- Karaca, 2011, Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction, Food Res. Int., 44, 2742, 10.1016/j.foodres.2011.06.012 · DOI · Paper page
- Arzeni, 2012, Comparative study of high intensity ultrasound effects on food proteins functionality, J. Food Eng., 108, 463, 10.1016/j.jfoodeng.2011.08.018 · DOI · Paper page
- Hu, 2013, Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions, Food Hydrocoll., 30, 647, 10.1016/j.foodhyd.2012.08.001 · DOI · Paper page
- Morales, 2015, Modification of foaming properties of soy protein isolate by high ultrasound intensity: particle size effect, Ultrason. Sonochem., 26, 48, 10.1016/j.ultsonch.2015.01.011 · DOI · Paper page
- O’Sullivan, 2016, The effect of ultrasound treatment on the structural, physical and emulsifying properties of animal and vegetable proteins, Food Hydrocoll., 53, 141, 10.1016/j.foodhyd.2015.02.009 · DOI · Paper page
- Xiong, 2016, High intensity ultrasound modified ovalbumin: structure, interface and gelation properties, Ultrason. Sonochem., 31, 302, 10.1016/j.ultsonch.2016.01.014 · DOI
- Güzey, 2006, Interfacial properties and structural conformation of thermosonicated bovine serum albumin, Food Hydrocoll., 20, 669, 10.1016/j.foodhyd.2005.06.008 · DOI
- Qu, 2018, Effects of ultrasonic and graft treatments on grafting degree, structure, functionality, and digestibility of rapeseed protein isolate-dextran conjugates, Ultrason. Sonochem., 42, 250, 10.1016/j.ultsonch.2017.11.021 · DOI
- Jiang, 2014, Effects of ultrasound on the structure and physical properties of black bean protein isolates, Food Res. Int., 62, 595, 10.1016/j.foodres.2014.04.022 · DOI · Paper page
- O’Sullivan, 2015, Comparative assessment of the effect of ultrasound treatment on protein functionality pre- and post-emulsification, Colloids Surfaces A Physicochem. Eng. Asp., 484, 89, 10.1016/j.colsurfa.2015.07.065 · DOI
- Maforimbo, 2001, In vitro relative protein digestibility and lipoxygenase activity used as parameters to test and compare quality in five varieties of soybean meals, J. Food Technol. Afr., 6, 48
- Saunders, 1973, Measurement of digestibility of alfalfa protein concentrates by in vivo and in vitro methods, J. Nutr., 103, 530, 10.1093/jn/103.4.530 · DOI
- Hsu, 1977, A multienzyme technique for estimating protein digestibility, J. Food Sci., 42, 1269, 10.1111/j.1365-2621.1977.tb14476.x · DOI · Paper page
- Elsohaimy, 2015, Physicochemical and functional properties of quinoa protein isolate, Ann. Agric. Sci., 60, 297, 10.1016/j.aoas.2015.10.007 · DOI · Paper page
- Tovar-Benítez, 2016, Microencapsulation of bayo bean (Phaseolus vulgaris) protein hydrolysate with inhibitory activity on angiotensin-i converting enzyme through freeze-drying, Rev. Mex. Ing. Quim., 15, 797, 10.24275/rmiq/Alim1038 · DOI
- Beck, 2017, Effect of different heat-treatment times and applied shear on secondary structure, molecular weight distribution, solubility and rheological properties of pea protein isolate as investigated by capillary rheometry, J. Food Eng., 208, 66, 10.1016/j.jfoodeng.2017.03.016 · DOI
- Mune, 2016, Production and characterization of cowpea protein hydrolysate with optimum nitrogen solubility by enzymatic hydrolysis using pepsin, J. Sci. Food Agric., 97, 2561, 10.1002/jsfa.8076 · DOI
- Indrawati, 2008, Characterization of protein stabilized foam formed in a continuous shear mixing apparatus, J. Food Eng., 88, 456, 10.1016/j.jfoodeng.2008.03.003 · DOI
- Vernon-Carter, 2001, Effect of foaming agents on the stability, rheological properties, drying kinetics and flavour retention of tamarind foam-mats, Food Res. Int., 34, 587, 10.1016/S0963-9969(01)00076-X · DOI
- Jambrak, 2009, Physical properties of ultrasound treated soy proteins, J. Food Eng., 93, 386, 10.1016/j.jfoodeng.2009.02.001 · DOI · Paper page
- Liu, 2016, Effect of ultrasonic processing on the changes in activity, aggregation and the secondary and tertiary structure of polyphenol oxidase in oriental sweet melon (Cucumis melo var. makuwa Makino), J. Sci. Food Agric., 97, 1326, 10.1002/jsfa.7869 · DOI
- Kang, 2016, Effects of power ultrasound on oxidation and structure of beef proteins during curing processing, Ultrason. Sonochem., 33, 47, 10.1016/j.ultsonch.2016.04.024 · DOI · Paper page
- Zhao, 2009, Interactions between bovine serum albumin and alginate: an evaluation of alginate as protein carrier, J. Colloid Interface Sci., 332, 345, 10.1016/j.jcis.2008.12.048 · DOI
- Martínez, 2011, Effect of dynamic high-pressure treatment on the interfacial and foaming properties of soy protein isolate-hydroxypropylmethylcelluloses systems, Food Hydrocoll., 25, 1640, 10.1016/j.foodhyd.2011.02.013 · DOI
- Zisu, 2013, Application of ultrasound to reduce viscosity and control the rate of age thickening of concentrated skim milk, Int. Dairy J., 31, 41, 10.1016/j.idairyj.2012.04.007 · DOI
- De Maria, 2017, Effects of high hydrostatic pressure on the enzymatic hydrolisis of bovine serum albumin, J. Sci. Food Agric., 97, 3151, 10.1002/jsfa.8157 · DOI
- Wang, 2011, Effect of secondary structure determined by FTIR spectra on surface hydrophobicity of soybean protein isolate, Proc. Eng., 15, 4819, 10.1016/j.proeng.2011.08.900 · DOI
- Carbonaro, 2008, Application of Fourier transform infrared spectroscopy to legume seed flour analysis, Food Chem., 108, 361, 10.1016/j.foodchem.2007.10.045 · DOI
- Carbonaro, 2012, Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study, Amino Acids, 43, 911, 10.1007/s00726-011-1151-4 · DOI · Paper page
- Camino, 2011, Hydroxypropylmethylcellulose at the oil-water interface. Part I. Bulk behaviour and dynamic adsorption as affected by pH, Food Hydrocoll., 25, 1, 10.1016/j.foodhyd.2010.04.012 · DOI
- Tang, 2015, Dynamic adsorption and dilatational properties of BSA at oil/water interface: role of conformational flexibility, Food Hydrocoll., 43, 388, 10.1016/j.foodhyd.2014.06.014 · DOI
- Ruíz-Henestrosa, 2007, Interfacial and foaming characteristics of soy globulins as a function of pH and ionic strength, Colloids Surfaces A Physicochem. Eng. Asp., 309, 202, 10.1016/j.colsurfa.2007.01.030 · DOI
- Bolontrade, 2013, Amaranth proteins foaming properties: adsorption kinetics and foam formation—Part 1, Colloids Surf. B Biointerfaces, 105, 319, 10.1016/j.colsurfb.2012.12.039 · DOI
- Pérez, 2009, Surface dilatational properties of whey protein and hydroxypropyl-methyl-cellulose mixed systems at the air–water interface, J. Food Eng., 94, 274, 10.1016/j.jfoodeng.2009.03.019 · DOI
- Carbonaro, 2010, Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region, Amino Acids, 38, 679, 10.1007/s00726-009-0274-3 · DOI · Paper page
- Tan, 2015, Characterisation of improved foam aeration and rheological properties of ultrasonically treated whey protein suspension, Int. Dairy J., 43, 7, 10.1016/j.idairyj.2014.09.013 · DOI
- Walstra, 1993, Principles of emulsion formation, Chem. Eng. Sci., 48, 333, 10.1016/0009-2509(93)80021-H · DOI · Paper page
Cited by
Rahman, M. M., & Lamsal, B. P. (2021) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12709 · Cited by 438
Figueroa-González, J. J., Lobato-Calleros, C., Vernon-Carter, E. J., Aguirre-Mandujano, E., Alvarez-Ramirez, J., & Martínez-Velasco, A. (2022) · LWT · doi:10.1016/j.lwt.2021.112561 · Cited by 144
Self-citationMozafarpour, R., Koocheki, A., Sani, M. A., McClements, D. J., & Mehr, H. M. (2022) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2022.102768 · Cited by 91
Gulzar, S., Martín-Belloso, O., & Soliva-Fortuny, R. (2024) · Foods · doi:10.3390/foods13030376 · Cited by 60
Zhang, L., Wang, X., Hu, Y., Abiola Fakayode, O., Ma, H., Zhou, C., Hu, Z., Xia, A., & Li, Q. (2021) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2021.105803 · Cited by 53
Metadata
- Authors
- Martínez-Velasco, A., Lobato-Calleros, C., Hernández-Rodríguez, B. E., Román-Guerrero, A., Alvarez-Ramirez, J., & Vernon-Carter, E. J.
- Venue
- Ultrasonics Sonochemistry
- Publisher
- Elsevier BV
- Published
- 2018-06
- Volume
- 44
- Pages
- 97-105
- ISSN
- 1350-4177 (ISSN-L)
- OpenAlex
- W2790395471
- Cited by
- 320
- References
- 0
- FWCI
- 15.95
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- Funders
- Consejo Nacional de Ciencia y Tecnología
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: High intensity ultrasound treatment of faba bean (Vicia faba L.) protein: Effect on surface properties, foaming ability and structural changes. https://app.cochat.ai/papers/10.1016/j.ultsonch.2018.02.007
- The paper
- Martínez-Velasco, A., Lobato-Calleros, C., Hernández-Rodríguez, B. E., Román-Guerrero, A., Alvarez-Ramirez, J., & Vernon-Carter, E. J. (2018). High intensity ultrasound treatment of faba bean (Vicia faba L.) protein: Effect on surface properties, foaming ability and structural changes. Ultrasonics Sonochemistry. https://doi.org/10.1016/j.ultsonch.2018.02.007
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.