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Rice is an excellent source of protein, and has an adequate balance of amino acids with the exception of the essential amino acid lysine.
It may be significant that the amino acids deleted in the rice CA transit peptide compared with the dicotyledonous CA transit peptides are between amino acid residues 60 and 100 of spinach CA Table 1.
These effects may be due to complex actions of various components abundantly found in the rice, including γ-aminobutyric acid, dietary fiber, phytic acid and ferulic acid.
Our study suggests that high temperature during the early grain-filling period can result in an accelerated grain-filling process, reduced N accumulation and content in rice grains, and consequently reduced amino acid content in the grain.
Since rice is the main source of calories and protein intake for billions of people, enhancing essential amino acids in rice represents a tremendous challenge.
These results suggested that HP treatment induced alteration of distribution of free amino acids of rice grains via proteolysis and certain amino acids metabolism pathways.
Hence, the amino acid composition is consistent with that of rice 13 kDa rolamin.
Open accessJournal Article
W W K Koo, J B Lasekan 
01 Feb 2007-MINERVA Pediatrica
26 Citations
Fortification of rice proteins with these two limiting amino acids improves its protein quality.
In conclusion, the exogenous application of amino acids could significantly increased the accumulation of nitrogen and the content of essential amino acids in grain; improve the yield and quality of rice.
Book ChapterDOI
K. Wakasa, J. M. Widholm 
01 Jan 1991
7 Citations
One would think that rice could be improved in several ways by selecting for amino acid analog resistance since most resistant mutants overproduce the corresponding natural amino acid.

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Isolation of antimicrobial peptides from yeast
5 answers
The isolation of antimicrobial peptides from yeast, particularly Saccharomyces cerevisiae, has been extensively studied. Various studies have highlighted the potential of yeast peptides in exhibiting antibacterial activities against a range of pathogens, including foodborne and clinically relevant bacteria. Additionally, yeast peptide extracts have shown bioactive properties such as antihypertensive, antioxidant, and even cholesterol-lowering activities, making them promising candidates for dietary supplementation and functional foods. Furthermore, the process of obtaining yeast peptide extracts has been optimized to be scalable, low-cost, and sustainable, aligning with circular economy principles. These findings underscore the significant potential of yeast-derived peptides as valuable sources of bioactive compounds with diverse applications in antimicrobial and health-promoting fields.
Why does an increase in protein content result in a decrease in the spreading rate in cookies Gluten-free?
5 answers
An increase in protein content leads to a decrease in the spreading rate in gluten-free cookies due to the impact of different protein sources on dough rheology and cookie characteristics. Whey protein concentrate (WPC) and soy protein (SP) additions have been shown to affect dough properties, resulting in changes in cookie spread ratios. Similarly, the substitution of flour with proteins like pea, potato, egg white, and whey alters hydration properties and dough rheology, influencing cookie texture and dimensions. The formation of protein networks during baking affects the structural integrity of the dough, impacting the spread rate of the cookies. Therefore, the type and level of protein added play a crucial role in determining the spreading rate of gluten-free cookies.
What are molar extinction coefficients?
4 answers
Molar extinction coefficients refer to the measure of how strongly a substance absorbs light at a particular wavelength. These coefficients have been extensively studied across various organic compounds, proteins, amino acids, and other biomolecules. The values of molar extinction coefficients are influenced by factors such as energy, effective atomic number, and the nature of atoms present in the molecules. For instance, different amino acids exhibit varying molar extinction coefficients, with tryptophan having a significantly higher value compared to others. Experimental and theoretical studies have shown good agreement in determining these coefficients, highlighting their importance in understanding the light absorption properties of different substances across a wide range of photon energies.
How have mass spectrometry instruments evolved over time in the analysis of triple-negative breast cancer (TNBC)?
5 answers
Mass spectrometry (MS) instruments have evolved significantly in the analysis of triple-negative breast cancer (TNBC). High-resolution MS instruments like time-of-flight (TOF) and Orbitrap MS have become prominent due to their sensitivity and selectivity. Novel approaches, such as colloidosomes-coupled matrix-assisted laser desorption/ionization time-of-flight MS, have been developed for TNBC diagnosis, offering high sensitivity and accuracy with minimal sample consumption. Liquid chromatography-tandem MS assays have enabled the detection of specific lipid biomarkers for TNBC, distinguishing TNBC from controls with high sensitivity and specificity. Additionally, conductive spray polymer ionization MS combined with machine learning has facilitated rapid metabolic fingerprinting for TNBC diagnosis and serum screening with high sensitivity and specificity. These advancements showcase the continuous progress in MS technology for TNBC analysis.
Is any enzyme capable for decarboxylate 3,5-dihydrohybenzoate?
5 answers
Yes, enzymes capable of decarboxylating 3,5-dihydroxybenzoate have been identified. A 3,4-dihydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum JW/Z-1T was found to catalyze the decarboxylation of 3,4-dihydroxybenzoate. Additionally, a new oxidative decarboxylation pathway for 3,5-dibromo-4-hydroxybenzoate (DBHB) catabolism was discovered in Pigmentiphaga sp. strain H8, involving the enzyme OdcA that mediates the oxidative decarboxylation of DBHB to 2,6-dibromohydroquinone. These findings highlight the enzymatic capability for decarboxylating hydroxybenzoate compounds, shedding light on the diverse enzymatic pathways involved in the catabolism of such aromatic compounds.
Can acly be biotinylated?
5 answers
Yes, acyl can be biotinylated. Biotinylation is the process of attaching biotin to a molecule, and it is commonly used in various research applications. While biotinylation is often associated with proteins, it can also be applied to other molecules, including acyl compounds. Biotinylation can occur through in vitro chemical synthesis, where biotin is covalently linked to reactive functional groups on the molecule. Additionally, biotinylation techniques, such as amide bond formation, [3+2] cycloadditions, Staudinger ligation, and thioether formation, can be utilized to attach biotin to small molecules like acyl compounds. Therefore, acyl compounds can indeed undergo biotinylation, expanding the scope of molecules that can be labeled and studied using this versatile technique.
Are there examples of uncouplers that lower body temperature?
5 answers
Various uncouplers have been identified that can lower body temperature by dissipating energy as heat instead of producing ATP. For instance, the mitochondrial uncoupling protein 1 (UCP1) found in brown adipose tissue is crucial for generating heat during cold exposure to defend body temperature. Additionally, studies have explored the use of chemical uncouplers like dinitrophenol (DNP) to increase mitochondrial uncoupling, leading to a decrease in metabolic efficiency and potentially lowering body temperature. Moreover, recent research has introduced a novel mitochondrial uncoupler named BAM15, which selectively uncouples mitochondria without affecting the plasma membrane potential, showing promise in protecting against ischemia-reperfusion injury in kidneys and potentially influencing body temperature regulation. These examples highlight the role of uncouplers in modulating body temperature through mitochondrial uncoupling mechanisms.
What are the effect of vernalization, photoperid and plant height of grainn quality of durum?
5 answers
Vernalization, photoperiod, and plant height significantly impact the grain quality of durum wheat. Vernalization, particularly in cultivars like Inia and Kariega, led to higher grain yield and protein content. Photoperiod and temperature interactions influenced grain yield, number, kernel size, and protein content, with longer photoperiods and lower temperatures resulting in superior grain quality. Plant height, influenced by breeding efforts, showed a trend towards reduced height without compromising biomass, leading to improved partitioning and nitrogen harvest index, ultimately affecting grain protein percentage and gluten index positively. These factors collectively play crucial roles in enhancing the protein content, gluten quality, and overall grain characteristics of durum wheat, highlighting the importance of considering vernalization, photoperiod, and plant height in durum wheat cultivation for optimal grain quality.
Is ABCG2 a knotted homodimer?
4 answers
Yes, ABCG2 is a homodimeric ATP-binding cassette (ABC) transporter that plays a crucial role in multidrug resistance in cancer cells. Structural studies have revealed that ABCG2 forms a symmetric homodimer configuration, with a key amino acid residue, F439, being essential for both transport and binding of various substrates and inhibitors. Molecular dynamics simulations and docking studies have provided insights into the structural stability and drug-binding sites of the ABCG2 homodimer. Additionally, investigations using bimolecular fluorescence complementation have confirmed the formation of specific ABCG2 dimers, supporting the concept of ABCG2 functioning as a homodimer. These findings collectively highlight the homodimeric nature of ABCG2 and its significance in mediating drug resistance mechanisms in cancer cells.
What are the current research efforts on using amines for carbon capture and storage?
5 answers
Current research efforts on using amines for carbon capture and storage focus on enhancing efficiency and reducing energy requirements. Studies explore the use of nano-catalytic materials in solvents to minimize energy for solvent regeneration. Additionally, rigorous models are being developed to understand the dynamics of amine-based CO2 capture plants, aiming to optimize technical and economic performance. Amino acids are also being investigated as potential replacements for traditional alkanolamines due to their low toxicity and high CO2 capture efficiency. Furthermore, recent advancements highlight the potential of nano-fluids in improving absorption efficiency for carbon capture, offering enhanced mass transfer performance. These diverse research approaches aim to develop more efficient and cost-effective carbon capture and storage technologies using amines.
Amino acids in milk for kids and elderly
5 answers
Amino acids in milk play a crucial role in providing essential nutrients for children and the elderly. Milk and dairy products are rich sources of high-quality dietary protein, containing a balanced profile of amino acids, including essential ones like threonine, methionine, valine, isoleucine, leucine, phenylalanine, lysine, and tryptophan. These amino acids are vital for the formation and maintenance of body tissues, making milk an important component of a healthy diet for both children and the elderly. While the amino acid requirements for infants are often based on the amino acid composition of breast milk, there is a lack of separate recommendations for the elderly, with insufficient data available to determine specific requirements for this age group. Overall, milk serves as a valuable source of essential amino acids for both children and the elderly, supporting their nutritional needs.