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1.
Plant Foods Hum Nutr ; 56(4): 385-95, 2001.
Article in English | MEDLINE | ID: mdl-11678443

ABSTRACT

Fatty acid contents at different stages of maturity and physicochemical characteristics of oil extracted from mature seeds of four safflower cultivars (S208, S400, S541, and S303) were studied. Results indicated that for all cultivars both saturated and unsaturated fatty acid contents fluctuated with seed growth and development. Palmitic acid content decreased up to day 20 after which it started to increase for the S400, S541, and S303 cultivars, while for S208 it progressively decreased. Stearic acid fluctuated with seed growth and development. Oleic acid showed slight changes with seed growth and development, while linoleic acid decreased with seed growth and development for the S400, S541, and S303 cultivars while for S208 after day 30, it started to increase significantly. For all cultivars, glyceride contents varied among the cultivars with maximum values of 97.70, 2.80 and 0.20 for tri-, di- and monoglycerides, respectively. Physicochemical investigation of mature seed oils showed that the color, density, refractive index, free fatty acids, peroxide value, saponification value and unsaponifiable matter were similar for all cultivars while viscosity, iodine value, and acetone insoluble matter varied among the cultivars.


Subject(s)
Fatty Acids/analysis , Safflower Oil/chemistry , Seeds/chemistry , Seeds/growth & development , Chemical Phenomena , Chemistry, Physical , Glycerides/analysis , Linoleic Acid/analysis , Oleic Acid/analysis , Palmitic Acid/analysis , Stearic Acids/analysis
2.
J Agric Food Chem ; 49(4): 2030-6, 2001 Apr.
Article in English | MEDLINE | ID: mdl-11308363

ABSTRACT

To investigate the effect of polysaccharide attachment to proteins on the production of IgG and IgE, the genetic attachment of polysaccharide to lysozymes (G49N and R21T) using the yeast expression system (Saccharomyces cerevisiae AH 22) and the Maillard-type polysaccharide attachment to native lysozyme and soybean P34 protein were attempted. The production of IgG and IgE was investigated by using mice immunized with the protein-polysaccharide conjugates or native proteins. The attachment of polysaccharide to lysozyme using the yeast expression system greatly suppressed the production level of IgG and IgE. The attachment of polysaccharide to native lysozyme and soybean P34 protein using the Maillard-type reaction was also found to be effective in reducing the production level of IgE compared to IgG.


Subject(s)
Immunoglobulin E/biosynthesis , Immunoglobulin G/biosynthesis , Muramidase/immunology , Polysaccharides/physiology , Soybean Proteins/immunology , Electrophoresis, Polyacrylamide Gel , Food Hypersensitivity/immunology , Food Hypersensitivity/prevention & control , Gene Expression , Immunoglobulin E/chemistry , Immunoglobulin G/chemistry , Maillard Reaction , Muramidase/genetics , Muramidase/metabolism , Saccharomyces cerevisiae/metabolism , Saccharomyces cerevisiae/physiology , Soybean Proteins/genetics , Soybean Proteins/metabolism
3.
J Agric Food Chem ; 48(2): 571-5, 2000 Feb.
Article in English | MEDLINE | ID: mdl-10691677

ABSTRACT

To elucidate the molecular mechanism of the allergenicity of soybean P34 protein recognized as the most allergenic protein in soybean, the protein was expressed in Escherichia coli transformed with a plasmid carrying P34 cDNA. SDS-PAGE pattern showed that the molecular weight of the recombinant P34 was approximately 2 kDa less than that of the native soybean P34. The difference in the molecular mass between these two proteins could be due to the native P34 in soybean being glycosylated at position Asn(170), whereas the recombinant protein generated in E. coli lacks this post-translational modification. Immunoblot analysis showed that both soybean and recombinant P34 proteins cross-reacted not only with polyclonal and monoclonal antibodies produced against P34 and crude soybean protein but also with patients' sera. The results suggest that the recombinant P34 is immunologically reactive, indicating that both proteins have similar epitope structures. Thus, the recombinant P34 produced by the E. coli expression system can be used as a standard allergen for molecular design to reduce the allergenic structure.


Subject(s)
Allergens/immunology , Escherichia coli/metabolism , Soybean Proteins/immunology , Animals , Dermatitis, Atopic/immunology , Electrophoresis, Polyacrylamide Gel , Humans , Mice , Mice, Inbred C3H , Rabbits , Recombinant Proteins/immunology
4.
J Agric Food Chem ; 47(6): 2262-6, 1999 Jun.
Article in English | MEDLINE | ID: mdl-10794620

ABSTRACT

The emulsifying properties of native and N- and C-terminal-deleted phosvitin (protease digests) were compared after conjugation with galactomannan. The emulsifying properties of Maillard-type phosvitin-galactomannan conjugates were greatly improved, whereas those of the protease-digested phosvitin-galactomannan conjugates were not so dramatically improved. Phosvitin was highly glycosylated with galactomannan, whereas the protease-digested phosvitin conjugate consisting of a highly phosphorylated core peptide fragment was not. The results suggest that both N and C termini of the peptide moiety, digested by protease, were essential for the improvement of emulsifying properties of phosvitin-galactomannan conjugates. In addition, the role of N and C termini as anchors in oil droplets was supported from the comparative studies of native phosvitin, phosvitin-galactomannan conjugates, and protease-digested phosvitin-galactomannan conjugates.


Subject(s)
Excipients , Mannans/chemistry , Phosvitin/chemistry , Amino Acid Sequence , Chymotrypsin , Galactose/analogs & derivatives , Glycosylation , Maillard Reaction , Molecular Sequence Data
5.
Plant Foods Hum Nutr ; 52(2): 161-70, 1998.
Article in English | MEDLINE | ID: mdl-9839815

ABSTRACT

Investigation of four safflower (Carthamus tinctorius L.) cultivars (S208, S400, S541 and S303) showed that when the seeds were harvested at different stages of growth and development (10, 20, 30, and 40 days) after flowering, moisture content significantly decreased with time. Oil, protein, ash and crude fiber were increased up to day 30. Thereafter, these parameters started to decline gradually with time. The cultivars differed in their final values; oil content of the seeds varied from 10.90 to 45.40%, moisture varied from 4.20 to 8.10% and from 8.50 to 11.10%, protein from 12.10 to 20.30% and from 13.40 to 29.60%, ash from 2.30 to 5.40% and from 2.80 to 6.50%, for the seeds and defatted meal, respectively. Crude fiber for the defatted meal was found to vary from 29.50 to 38.60%. Carbohydrate for all cultivars decreased rapidly up to day 40 with final values varying from 28.10 to 63.30% and from 56.70 to 70.30% for the seeds and defatted meal, respectively. Mineral content (Cu, Zn, Fe, Mg, Mn) fluctuated while phosphorus content significantly increased with time for all cultivars. Amino acid content of the defatted meal increased with time up to day 30 after which it started to decline gradually for all cultivars.


Subject(s)
Amino Acids/analysis , Minerals/analysis , Seeds/chemistry , Seeds/growth & development , Carbohydrates/analysis , Dietary Fiber/analysis , Phosphorus/analysis , Plant Proteins/analysis , Safflower Oil/analysis
6.
Plant Foods Hum Nutr ; 47(3): 257-63, 1995 Apr.
Article in English | MEDLINE | ID: mdl-7659703

ABSTRACT

A field investigation of two faba bean cultivars (cv.), Agabat and Silaim, showed that bean yellow mosaic virus (BYMV) infection reduced (p < or = 0.001) yield (Kg/ha), protein content and in vitro protein digestibility (IVPD) but increased (p < or = 0.05) tannin content (mg/100 ml). Nitrogen fertilization with viral infection significantly reduced yield and IVPD for cv. Silaim and increased (p < or = 0.05) protein and tannin contents. Nitrogen fertilization alone was found to increase (p < or = 0.05) yield, protein and tannin contents but slightly reduced IVPD. Rhizobium inoculation with viral infection significantly decreased yield per unit area, protein content and IVPD, but increased (p < or = 0.05) tannin content. Rhizobium inoculation alone significantly increased (p < or = 0.001) yield and tannin content and slightly increased protein content but decreased IVPD. The results indicated that nitrogen fertilization or nitrogen fixation increased yield, protein and tannin contents and decreased IVPD. Viral infection had an adverse effect on yield, protein content and IVPD but had no effect on tannin content.


Subject(s)
Fabaceae , Fertilizers , Hydrolyzable Tannins/metabolism , Nitrogen Fixation , Nitrogen/administration & dosage , Plant Viruses , Plants, Medicinal , Digestion , Fabaceae/metabolism , Fabaceae/virology , In Vitro Techniques , Plant Diseases , Plant Proteins/metabolism
7.
Plant Foods Hum Nutr ; 44(2): 119-30, 1993 Sep.
Article in English | MEDLINE | ID: mdl-8378270

ABSTRACT

Two faba bean cultivars (317/99/81 and Giza/402) obtained from Shambat Research Station in Northern Sudan, were used for this study. Investigation showed that the tannin contents of untreated seeds were 0.077% and 0.067% for cultivars 317/99/81 and Giza/402. In vitro protein digestibility values were 80.68% and 81.48% for the two cultivars, respectively. The extractable tannin content of the faba bean cultivars was markedly reduced by imbibing water or Na2CO3 solution into whole seeds and incubating them at 30 degrees C for 1, 3, 6, 12 or 24 hours, or at 100 degrees C for 5, 10 or 20 minutes. The extent of reduction depended on time, temperature, and Na2CO3 concentration; the percent tannin extracted and percent in vitro protein digestibility increased with time or Na2CO3 concentration, while application of high temperature reduced the time.


Subject(s)
Carbonates/pharmacology , Fabaceae/chemistry , Hydrolyzable Tannins/analysis , Plant Proteins/metabolism , Plants, Medicinal , Seeds/chemistry , Digestion , Kinetics , Pancreatin/metabolism , Sudan , Temperature
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