ABSTRACT
The effect of power, time and temperature of ultrasound on the structure of ß-conglycinin (7S) and glycinin (11S), and on the antioxidant activity of their hydrolysates were investigated. All ultrasound treated 7S and 11S fractions showed an increase in the α-helix and ß-turn proportions, and a decrease in ß-sheet and random coil proportions. The polarity of 7S and 11S microenvironment increased after ultrasound treatment. Ultrasound treatment significantly increased the reduction capacity and iron chelating capacity of 7S and 11S hydrolysates. The degree of hydrolysis and free SH groups of 7S and 11S hydrolysates increased after ultrasound pre-treatment. The relative content of high molecular weight peptides reduced, and the relative content of low molecular weight peptides increased in ultrasound treated 7S and 11S hydrolysates. The ultrasonication exposed certain groups of 7S and 11S fractions, improved contact with enzymes, and increased the content of highly active soybean antioxidant peptides.
Subject(s)
Antigens, Plant/chemistry , Antioxidants/metabolism , Globulins/chemistry , Glycine max/chemistry , Plant Extracts/chemistry , Seed Storage Proteins/chemistry , Soybean Proteins/chemistry , Ultrasonics , Antigens, Plant/radiation effects , Antioxidants/analysis , Globulins/radiation effects , Oxidation-Reduction , Plant Extracts/isolation & purification , Plant Extracts/radiation effects , Seed Storage Proteins/radiation effects , Soybean Proteins/radiation effects , TemperatureABSTRACT
The present work describes radiation—induced effects on seed composition vis—à—vis total seed proteins, antioxidant levels and protein profiling employing two dimensional gel electrophoresis (2D—GE) in kabuli and desi chickpea varities. Seeds were exposed to the radiation doses of 1,2,3,4 and 5 kGy. The total protein concentrations decreased and antioxidant levels were increased with increasing dose compared to control seed samples. Radiation induced effects were dose dependent to these seed parameters while it showed tolerance to 1 kGy dose. Increase in the dose was complimented with increase in antioxidant levels, like 5 kGy enhanced % scavenging activities in all the seed extracts. Precisely, the investigations reflected that the dose range from 2 to 5 kGy was effective for total seed storage proteins, as depicted quantitatively and qualitative 2D—GE means enhance antioxidant activities in vitro.
Subject(s)
Antioxidants/metabolism , Cicer/radiation effects , Gamma Rays/adverse effects , Seed Storage Proteins/radiation effects , Seeds/radiation effects , Antioxidants/radiation effects , Cicer/classification , Electrophoresis, Gel, Two-Dimensional , Gene Expression ProfilingABSTRACT
Non-invasive techniques are a key to study nutrition and structure interaction. Fourier transform infrared microspectroscopy coupled with a synchrotron radiation source (SR-IMS) is a rapid, non-invasive, and non-destructive bioanalytical technique. To understand internal structure changes in relation to nutrient availability in oil seed processing is vital to find optimal processing conditions. The objective of this study was to use a synchrotron-based bioanalytical technique SR-IMS as a non-invasive and non-destructive tool to study the effects of heat-processing methods and oil seed canola type on modeled protein structure based on spectral data within intact tissue that were randomly selected and quantify the relationship between the modeled protein structure and protein nutrient supply to ruminants. The results showed that the moisture heat-related processing significantly changed (p<0.05) modeled protein structures compared to the raw canola (control) and those processing by dry heating. The moisture heating increased (p<0.05) spectral intensities of amide I, amide II, α-helices, and ß-sheets but decreased (p<0.05) the ratio of modeled α-helices to ß-sheet spectral intensity. There was no difference (p>0.05) in the protein spectral profile between the raw and dry-heated canola tissue and between yellow- and brown-type canola tissue. The results indicated that different heat processing methods have different impacts on the protein inherent structure. The protein intrinsic structure in canola seed tissue was more sensitive and more response to the moisture heating in comparison to the dry heating. These changes are expected to be related to the nutritive value. However, the current study is based on limited samples, and more large-scale studies are needed to confirm our findings.
Subject(s)
Brassica napus/chemistry , Brassica rapa/chemistry , Dietary Proteins/chemistry , Food Handling , Seed Storage Proteins/chemistry , Seeds/chemistry , Animal Feed/analysis , Animal Feed/radiation effects , Animals , Brassica napus/radiation effects , Brassica rapa/radiation effects , Dietary Proteins/radiation effects , Hot Temperature/adverse effects , Humans , Microchemistry/methods , Molecular Imaging/methods , Nutritive Value , Protein Stability/radiation effects , Protein Structure, Secondary/radiation effects , Ruminants , Seed Storage Proteins/radiation effects , Seeds/radiation effects , Spectroscopy, Fourier Transform Infrared , SynchrotronsABSTRACT
Physical and biochemical analysis of protein polymorphisms in seed storage proteins of a mutant population of sorghum revealed a mutant with redirected accumulation of kafirin proteins in the germ. The change in storage proteins was accompanied by an unusually high level accumulation of free lysine and other essential amino acids in the endosperm. This mutant further displayed a significant suppression in the synthesis and accumulation of the 27kDa γ-, 24kDa α-A1 and the 22kDa α-A2 kafirins in the endosperm. The suppression of kafirins was counteracted by an upsurge in the synthesis and accumulation of albumins, globulins and other proteins. The data collectively suggest that sorghum has huge genetic potential for nutritional biofortification and that induced mutations can be used as an effective tool in achieving premium nutrition in staple cereals.
