Foaming Properties of Soy Protein Isolate Hydrolysates

Luis Alberto Panizzolo; María Cristina Añón

doi:doi:10.11648/j.jfns.20150301.11

| Peer-Reviewed

Foaming Properties of Soy Protein Isolate Hydrolysates

Luis Alberto Panizzolo, María Cristina Añón

Published in Journal of Food and Nutrition Sciences (Volume 3, Issue 1)

Received: 26 November 2014 Accepted: 22 December 2014 Published: 4 January 2015

Views: Downloads:

Download PDF

Share This Article

Twitter
Linked In
Facebook

Abstract

Tensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and physicochemically, and their foam-forming and -stabilizing capacity studied. Protein structural changes upon reaction ending were correlated with functional and interfacial properties and with the behaviour thereof with varying hydrolysis degree. Two different means of halting hydrolysis -pH reduction (pH=2) and quick freezing (-18 ºC), respectively- were studied. Distinct structural changes and associated functional properties were found according to reaction ending conditions. No improvement of foaming properties was found for partially-hydrolyzed isolates subject to freezing at reaction ending - with respect to the starting unhydrolyzed soy protein isolate. In contrast, pH treatment as a means of halting hydrolysis led to a significant enhancement of the foaming properties of soybean protein hydrolysates consistently for all studied hydrolysis degrees (0%, 1.8%, 2.5% and 6%).

Published in	Journal of Food and Nutrition Sciences (Volume 3, Issue 1)
DOI	10.11648/j.jfns.20150301.11
Page(s)	1-9
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2015. Published by Science Publishing Group

Keywords

Soy Protein, Enzymatic Hydrolysis, Foaming Properties

References

[1]	van Vliet, T.; Martin, A. H. & Bos, M. A. (2002). Gelation and interfacial behaviour of vegetable proteins. Current Opininion in Colloid & Interface Science. 7, 462 - 468.
[2]	Damodaran, S. (2005). Protein stabilization of emulsions and foams. Journal of Food Science. 70, 54 – 66.
[3]	Schwenke, K. D. (2001). Reflections about the functional potential of legume proteins. A review. Nahrung. 45, 377-381.
[4]	Were, L.; Hettiarachchy, N. S. & Kalapathy, U. (1997). Modified Soy proteins with improved foaming and water hydration properties. Journal of Food Science. 62, 821-824.
[5]	Wu, W.; Hettiarachchy, N. S. & Qi, M. (1998). Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration. Journal of the American Oil of Chemists’ Society. 75, 845-850.
[6]	Petruccelli, S. & Añón, M. C. (1994). The realtionship between the method of preparation and the structural and functional properties of soy protein isolates. Part I: Structural and hydration properties. Journal of Agriculture and Food Chemistry. 42, 2161-2169.
[7]	Adler-Nissen, J. (1976). Enzymic hydrolysis of proteins for increased solubility. Journal of Agricultural and Food Chemistry. 24, 1090 – 1093.
[8]	Cayot, P., & Tainturier, G. (1997). The quantification of protein amino groups by the trinitrobenzenesulfonic acid method: a reexamination. Analytical Biochemistry. 249, 184-200.
[9]	Lowry, O. H.; Rosembroug, H. J.; Lewis, A. & Randall, R. J. (1951). Protein measurement with the folin phenol reagent. Journal of Biological Chemistry. 193, 265–275.
[10]	AOAC. (1975). Official methods of analysis. Washington: Association of Official Analytical Chemists.
[11]	Hayakawa, S. & Nakai, S. (1985). Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science. 50, 486-491.
[12]	Kato, A. & Nakai, S. (1980). Hydrophobicity determined by fluorescence probe method and its correlation with surface properties of proteins. Biochimica et Biophysica Acta. 624; 13-20.
[13]	Petruccelli, S. & Añón, M. C. (1995). Thermal aggregation of soy protein isolate. Journal Agriculture Food Chemistry. 43, 3035-3042.
[14]	Panizzolo, L. A.; Mussio, L. E. y Añón, M. C. 2014. A kinetic model for describing the effect of proteins on the air-water interface tension. Journal of Food Science and Engineering. (in press).
[15]	Loisel, W.; Guéguen, J. & Popineau, Y. (1993). A new apparatus for analyzing foaming properties of proteins. In K. D. Schwenke, & R. Mothes, Food Proteins. Structure and functionality (pp320-323). Weinheim: VCH.
[16]	Wagner, J. R.; Sorgentini, D. A. & Añón, M. C. (1996). Thermal and electrophoretic behavior, hydrophobity and some functional properties of acid-treatred soy isolates. Journal of Agricultural and Food Chemistry. 44, 1881-1889.
[17]	Panizzolo, L. A.; Mussio, L. E. y Añón, M. C. (2012). A kinetic description for the destabilization process of protein foams. International Journal of Food Properties. 15 (1), 60-68.
[18]	Molina Ortiz, S. E. (1997). Modificación enzimática de propiedades funcionales de aislados proteicos de soja. Tesis, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, Argentina.
[19]	Wagner, J. R. & Añón, M. C. (1990). Influence of denaturation, hydrophobicity and sulfhidryl content on solubility and water absorbing capacity of soy protein isolate. Journal of Food Science. 50, 765-770
[20]	Puppo, M. C. & Añón, M. C. (1999). Soybean protein dispersions at acid pH. Thermal and rheological properties. Journal of Food Science. 64, 50-56.
[21]	Schwenke, K. D.; Staatz, A.; Dudek, S.; Krause, J. P. & Noack, J. (1995). Legumin-T from faba bean legumin: isolation, partial characterization and surface functional properties. Nahrung. 39, 193-.202.
[22]	Koshiyama, I. (1972). Comparison of acid induced conformation changes between 7S and 11S globulin in soybean seeds. Journal of the Science of Food and Agriculture. 23, 853-859.
[23]	Martin, A. H.; Bos, M. A. & van Vliet, T. (2002). Interfacial rheological properties and conformational aspects of soy glycinin at the air_water interface. Food Hydrocolloids. 16, 63-71.
[24]	Garofalakis, G. & Murray, B. S. (2001). Dilatational rheology and foaming properties of sucrose monoesters in the presence of b-lactoglobulin. Colloids and Surfaces B Biointerfaces. 21, 3–17.
[25]	Damodaran, S. (1996). Amino acids, peptides, and proteins. In O. R. Fennema, Food Chemistry (pp 321–429). New York: Marcel Dekker.
[26]	Graham, D. E. & Phillips, M. C. (1976). The conformation of proteins at the air-water interface and their role in stabilizing foams. In Foam, editado por Akers, R. J. Academic Press, New York. 237-255.
[27]	Phillips, L. G. (1981). Protein conformation at liquid interfaces and its role in stabilizing emulsions and foams. Food Technology. 35, 50-57.
[28]	Kinsella, J. E. (1981). Relationship between structure and functional properties of food proteins. In P. F. Fox, & J. J. Condon. Food Proteins. London: Applied Science Publishers.
[29]	Cheftel, J. C., Cuq J. L., & Lorient, D. (1985). Aminoacids, Peptides and Proteins. In O. R. Fennema, Food Chemistry (pp 245-369). New York: Marcel Dekker.
[30]	Damodaran, S. (1997). Protein-stabilized foams and emulsions. In S. Damodaran, & A. Paraf. Food proteins and their applications (pp 57–110). New York: Marcel Dekker,
[31]	Hill, S. E. (1998). Emulsions and foams. In S. E. Hill, D. A. Ledward, & J. R. Mitchell. Fuctional properties of food macromolecules (pp 302-334). Maryland: Aspen Publishers, Inc.
[32]	Sorgentini, D. A.; Wagner, J. R. & Añón, M. C. (1995). Effects of thermal treatment of soy protein isolate on the characteristics and structure: function relationship of soluble and insoluble fractions. Journal of Agriculture and Food Chemistry. 43, 2471-2479.
[33]	Walstra, P. (1996). Dispersed systems: basic considerations. In O. R. Fennema, Food Chemistry (pp 95–155). New York: Marcel Dekker.
[34]	Halling, P.J. (1981). Protein stabilized foam and emulsions. CRC Critical Reviews in Food Science and Nutrition. 15: 155-203.
[35]	Salager, J. L.; Andérez, J. M. & Forgiarini, A. (2003). Influencia de la formulación sobre las espumas. Cuaderno Firp 263-A. Universidad de Los Andes, Mérida, Venezuela.
[36]	Manev, E. D.; Sazdanova, S. V. & Wasan, D. T. (1984). Emulsion and foam stability: the effect of film size on film drainage, Journal of Colloid and Interface Science. 97, 591–594.

Cite This Article

Plain Text BibTeX RIS

APA Style

Luis Alberto Panizzolo, María Cristina Añón. (2015). Foaming Properties of Soy Protein Isolate Hydrolysates. Journal of Food and Nutrition Sciences, 3(1), 1-9. https://doi.org/10.11648/j.jfns.20150301.11

Copy | Download

ACS Style

Luis Alberto Panizzolo; María Cristina Añón. Foaming Properties of Soy Protein Isolate Hydrolysates. J. Food Nutr. Sci. 2015, 3(1), 1-9. doi: 10.11648/j.jfns.20150301.11

Copy | Download

AMA Style

Luis Alberto Panizzolo, María Cristina Añón. Foaming Properties of Soy Protein Isolate Hydrolysates. J Food Nutr Sci. 2015;3(1):1-9. doi: 10.11648/j.jfns.20150301.11

Copy | Download

@article{10.11648/j.jfns.20150301.11,
  author = {Luis Alberto Panizzolo and María Cristina Añón},
  title = {Foaming Properties of Soy Protein Isolate Hydrolysates},
  journal = {Journal of Food and Nutrition Sciences},
  volume = {3},
  number = {1},
  pages = {1-9},
  doi = {10.11648/j.jfns.20150301.11},
  url = {https://doi.org/10.11648/j.jfns.20150301.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.jfns.20150301.11},
  abstract = {Tensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and physicochemically, and their foam-forming and -stabilizing capacity studied. Protein structural changes upon reaction ending were correlated with functional and interfacial properties and with the behaviour thereof with varying hydrolysis degree. Two different means of halting hydrolysis -pH reduction (pH=2) and quick freezing (-18 ºC), respectively- were studied. Distinct structural changes and associated functional properties were found according to reaction ending conditions. No improvement of foaming properties was found for partially-hydrolyzed isolates subject to freezing at reaction ending - with respect to the starting unhydrolyzed soy protein isolate. In contrast, pH treatment as a means of halting hydrolysis led to a significant enhancement of the foaming properties of soybean protein hydrolysates consistently for all studied hydrolysis degrees (0%, 1.8%, 2.5% and 6%).},
 year = {2015}
}

Copy | Download

TY  - JOUR
T1  - Foaming Properties of Soy Protein Isolate Hydrolysates
AU  - Luis Alberto Panizzolo
AU  - María Cristina Añón
Y1  - 2015/01/04
PY  - 2015
N1  - https://doi.org/10.11648/j.jfns.20150301.11
DO  - 10.11648/j.jfns.20150301.11
T2  - Journal of Food and Nutrition Sciences
JF  - Journal of Food and Nutrition Sciences
JO  - Journal of Food and Nutrition Sciences
SP  - 1
EP  - 9
PB  - Science Publishing Group
SN  - 2330-7293
UR  - https://doi.org/10.11648/j.jfns.20150301.11
AB  - Tensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and physicochemically, and their foam-forming and -stabilizing capacity studied. Protein structural changes upon reaction ending were correlated with functional and interfacial properties and with the behaviour thereof with varying hydrolysis degree. Two different means of halting hydrolysis -pH reduction (pH=2) and quick freezing (-18 ºC), respectively- were studied. Distinct structural changes and associated functional properties were found according to reaction ending conditions. No improvement of foaming properties was found for partially-hydrolyzed isolates subject to freezing at reaction ending - with respect to the starting unhydrolyzed soy protein isolate. In contrast, pH treatment as a means of halting hydrolysis led to a significant enhancement of the foaming properties of soybean protein hydrolysates consistently for all studied hydrolysis degrees (0%, 1.8%, 2.5% and 6%).
VL  - 3
IS  - 1
ER  -

Copy | Download

Author Information

Luis Alberto Panizzolo

Departamento de Ciencia y Tecnología de Alimentos, Facultad de Química, Universidad de la República, Av. Gral, Flores 2124, 11800, Montevideo, Uruguay
María Cristina Añón

Download PDF

Sections

Plain Text BibTeX RIS

APA Style

Luis Alberto Panizzolo, María Cristina Añón. (2015). Foaming Properties of Soy Protein Isolate Hydrolysates. Journal of Food and Nutrition Sciences, 3(1), 1-9. https://doi.org/10.11648/j.jfns.20150301.11

Copy | Download

ACS Style

Luis Alberto Panizzolo; María Cristina Añón. Foaming Properties of Soy Protein Isolate Hydrolysates. J. Food Nutr. Sci. 2015, 3(1), 1-9. doi: 10.11648/j.jfns.20150301.11

Copy | Download

AMA Style

Luis Alberto Panizzolo, María Cristina Añón. Foaming Properties of Soy Protein Isolate Hydrolysates. J Food Nutr Sci. 2015;3(1):1-9. doi: 10.11648/j.jfns.20150301.11

Copy | Download

@article{10.11648/j.jfns.20150301.11,
  author = {Luis Alberto Panizzolo and María Cristina Añón},
  title = {Foaming Properties of Soy Protein Isolate Hydrolysates},
  journal = {Journal of Food and Nutrition Sciences},
  volume = {3},
  number = {1},
  pages = {1-9},
  doi = {10.11648/j.jfns.20150301.11},
  url = {https://doi.org/10.11648/j.jfns.20150301.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.jfns.20150301.11},
  abstract = {Tensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and physicochemically, and their foam-forming and -stabilizing capacity studied. Protein structural changes upon reaction ending were correlated with functional and interfacial properties and with the behaviour thereof with varying hydrolysis degree. Two different means of halting hydrolysis -pH reduction (pH=2) and quick freezing (-18 ºC), respectively- were studied. Distinct structural changes and associated functional properties were found according to reaction ending conditions. No improvement of foaming properties was found for partially-hydrolyzed isolates subject to freezing at reaction ending - with respect to the starting unhydrolyzed soy protein isolate. In contrast, pH treatment as a means of halting hydrolysis led to a significant enhancement of the foaming properties of soybean protein hydrolysates consistently for all studied hydrolysis degrees (0%, 1.8%, 2.5% and 6%).},
 year = {2015}
}

Copy | Download

TY  - JOUR
T1  - Foaming Properties of Soy Protein Isolate Hydrolysates
AU  - Luis Alberto Panizzolo
AU  - María Cristina Añón
Y1  - 2015/01/04
PY  - 2015
N1  - https://doi.org/10.11648/j.jfns.20150301.11
DO  - 10.11648/j.jfns.20150301.11
T2  - Journal of Food and Nutrition Sciences
JF  - Journal of Food and Nutrition Sciences
JO  - Journal of Food and Nutrition Sciences
SP  - 1
EP  - 9
PB  - Science Publishing Group
SN  - 2330-7293
UR  - https://doi.org/10.11648/j.jfns.20150301.11
AB  - Tensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and physicochemically, and their foam-forming and -stabilizing capacity studied. Protein structural changes upon reaction ending were correlated with functional and interfacial properties and with the behaviour thereof with varying hydrolysis degree. Two different means of halting hydrolysis -pH reduction (pH=2) and quick freezing (-18 ºC), respectively- were studied. Distinct structural changes and associated functional properties were found according to reaction ending conditions. No improvement of foaming properties was found for partially-hydrolyzed isolates subject to freezing at reaction ending - with respect to the starting unhydrolyzed soy protein isolate. In contrast, pH treatment as a means of halting hydrolysis led to a significant enhancement of the foaming properties of soybean protein hydrolysates consistently for all studied hydrolysis degrees (0%, 1.8%, 2.5% and 6%).
VL  - 3
IS  - 1
ER  -

Copy | Download