INVESTIGADORES
AÑON Maria Cristina
artículos
Título:
Analysis of products, mechanisms of reaction and some functional properties of soy protein hydrolysates
Autor/es:
MOLINA ORTIZ, S.E; AÑON. M.C
Revista:
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY (JAOCS)
Editorial:
SPRINGER
Referencias:
Año: 2000 vol. 77 p. 1293 - 1301
ISSN:
0003-021X
Resumen:
ABSTRACT: Soybean protein isolates were hydrolyzed with
papain, bromelain, cucurbita, hieronymin, and pomiferin. The
highest hydrolysis rate for cucurbita and the lowest for papain
was detected at 720 min. Gel filtration, reversed-phase liquid
chromatography, and electrophoresis showed that the action of
each protease was different. Pomiferin acted on the native structure
of â-conglycinin and glycinin, generating a large number
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
papain, bromelain, cucurbita, hieronymin, and pomiferin. The
highest hydrolysis rate for cucurbita and the lowest for papain
was detected at 720 min. Gel filtration, reversed-phase liquid
chromatography, and electrophoresis showed that the action of
each protease was different. Pomiferin acted on the native structure
of â-conglycinin and glycinin, generating a large number
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
papain, bromelain, cucurbita, hieronymin, and pomiferin. The
highest hydrolysis rate for cucurbita and the lowest for papain
was detected at 720 min. Gel filtration, reversed-phase liquid
chromatography, and electrophoresis showed that the action of
each protease was different. Pomiferin acted on the native structure
of â-conglycinin and glycinin, generating a large number
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
Soybean protein isolates were hydrolyzed with
papain, bromelain, cucurbita, hieronymin, and pomiferin. The
highest hydrolysis rate for cucurbita and the lowest for papain
was detected at 720 min. Gel filtration, reversed-phase liquid
chromatography, and electrophoresis showed that the action of
each protease was different. Pomiferin acted on the native structure
of â-conglycinin and glycinin, generating a large number
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).
â-conglycinin and glycinin, generating a large number
of small hydrolysis products with hydrophilic and hydrophobic
characteristics. The hydrolysates obtained with cucurbita
showed residual structures that were almost intact and very similar
to the substrate and contained a low number of small peptides.
The hydrolyzates obtained with papain, bromelain, and
hieronymin had hydrolysis products with structures similar to
the partially hydrolyzed native isolate. The molecular masses of
these products were similar to or lower than the controls.
Polypeptides of low molecular mass were also detected. The
prevalence of one-by-one and zipper mechanisms was suggested
for cucurbita and pomiferin, respectively. For the other
proteases both mechanisms were likely to coexist. The solubility
of hydrolysates and their ability to form and stabilize foams
correlated well with the structural properties and with the suggested
mechanisms of hydrolysis. The best properties were presented
by the hydrolysates prepared with cucurbita. Foaming
ability for pomiferin hydrolysates was as high as that for unhydrolyzed
soy isolate, but the foams were extremely unstable.
Paper no. J9469 in JAOCS 77, 12931301 (December 2000).JAOCS 77, 12931301 (December 2000).