Physicochemical Properties and Functionality of Rice Bran Protein Hydrolyzate Prepared from Heat-stabilized Defatted Rice Bran with the Aid of Enzymes

ABSTRACT: Molecular size, thermal properties, hydrophobicity, nitrogen solubility, and emulsifying and foaming properties were determined for protein products from heat‐stabilized defatted rice bran. The freeze‐dried and spray‐dried proteins had molecular sizes between 6.5 to 66.2 kDa; denaturation temperatures of 84.1 and 84.6 °C, enthalpies of 2.5 and 2.37 J/g, hydrophobicities of 20677 and 22611, maximum solubilities of 66.3% and 66.1% at pH 12.0, emulsifying capacities of 0.19 and 0.18, emulsion stabilities of 16.5 and 17.3 min, foam capacities of 4.0 mL and 4.2 mL, and negligible foam stabilities. These results demonstrated that the extracted rice bran protein has potential as a nutraceutical ingredient in food applications.     

Phenolic Profile and Antioxidant Activity of Extracts Prepared from Fermented Heat‐Stabilized Defatted Rice Bran

Heat‐stabilized, defatted rice bran (HDRB) serves as a potential source of phenolic compounds which have numerous purported health benefits. An estimated 70% of phenolics present in rice bran are esterified to the arabinoxylan residues of the cell walls. Release of such compounds could provide a value‐added application for HDRB. The objective of this study was to extract and quantify phenolics from HDRB using fermentation technology. Out of 8 organisms selected for rice bran fermentation, Bacillus subtilis subspecies subtilis had the maximum phenolic release of 26.8 mg ferulic acid equivalents (FAE) per gram HDRB. Response surface methodology was used to further optimize the release of rice bran phenolics. An optimum of 28.6 mg FAE/g rice bran was predicted at 168 h, 0.01% inoculation level, and 100 mg HDRB/mL. Fermentation of HDRB for 96 h with B. subtilis subspecies subtilis resulted in a significant increase in phenolic yield, phenolic concentration, and radical scavenging capacity. Fermented rice bran had 4.86 mg gentistic acid, 1.38 mg caffeic acid, 6.03 mg syringic acid, 19.02 mg (‐)‐epicatechin, 4.08 mg p‐courmaric acid, 4.64 mg ferulic acid, 10.04 mg sinapic acid, and 17.59 mg benzoic acid per 100 g fermented extract compared to 0.65 mg p‐courmaric acid and 0.36 mg ferulic acid per 100 g nonfermented extract. The high phenolic content and antioxidant activity of fermented HDRB extract indicates that rice bran fermentation under optimized condition is a potential means of meeting the demand for an effective and affordable antioxidant.     

Characteristics and Functionality Enhancement by Glycosylation of Bitter Melon (Momordica charantia) Seed Protein

Seeds of ripe bitter melon (Momordica charantia) contain approximately 30% protein. However, this protein, which is less functional than soy protein, may have desirable functionalities as a food ingredient after modification. Bitter melon seed protein isolate (BMSPI) was prepared under optimal extraction conditions (defatted meal to 1.3 M NaCl was 1:10 w/v; pH 9.0) and its functional properties were investigated before and after modification by glycosylation. Glycosylation was conducted at varying relative humidities (50%/65%/80%) and temperatures (40 °C/50 °C/60 °C) using a response surface central composite design. Degree of glycosylation (DG) ranged from 39.3 to 52.5%, 61.7 to 70.9%, and 81.2 to 94.8% at 40 °C, 50 °C, and 60 °C, respectively (P values < 0.0001). Denaturation temperatures of all DGs ranged from 111.6 °C to 114.6 °C, while unmodified/native BMSPI had a value of 113.2 °C. Surface hydrophobicity decreased to approximately 60% when the DG was maximal (94.8%). Solubility decreased almost 90% when the DG was maximal in comparison to the native BMSPI (62.0%). Emulsifying activity increased from 0.35 to 0.80 when the DGs were ≥80%, while emulsion stability increased from 63 to 72 min when the DGs were greater than 70%. A similar trend was observed with foaming capacity and foaming stability of the glycosylated proteins. This glycosylated BMSPI with improved emulsifying and foaming properties could be used as an ingredient in food products where such properties are required.     

Amino Acid Profiles of 44 Soybean Lines and ACE‐I Inhibitory Activities of Peptide Fractions from Selected Lines

Soybeans are cultivated in the United States chiefly for cooking oil, while the residue after oil extraction (soybean meal) is mostly used in animal feed formulations. High protein content in the defatted soybean meals led to the extraction of pure protein and its application in food products. We selected 44 soybean lines to determine their moisture and protein contents, and their amino acid composition was investigated. Soybean lines with high protein content, one high yielding (R95‐1705), and two high oleic acid (N98‐4445A, S03‐543CR), were selected for protein isolate preparation, hydrolysis using alcalase and gastro‐intestinal (GI) resistance. Furthermore, the GI resistant hydrolysates were fractionated and tested for angiotensin‐I‐converting enzyme (ACE‐I) inhibition activity. The amino acid analysis showed high methionine in the high protein and fatty acid lines (R05‐4494 and R05‐5491), and high cysteine content in one of the high oleic acid soybean line CRR05‐188 in comparison to the check lines (UA‐4805 and 5601‐T). The protein isolate with the highest purity (90–93 %) was derived from the selected lines N98‐4445A and S03‐543CR, and hydrolyzed using alcalase enzyme. The protein hydrolysates (500 µg/mL) showed inhibition of the ACE‐I by 49 %. The results from this study will promote the use of high oleic acid soybeans as a source of protein and peptides with functional activities.     

Protein extraction optimisation,characterisation, and functionalities of protein isolate from bitter melon (Momordica charantia) seed

Bitter melon seeds are a rich source of protein. Optimum conditions for protein extraction from the seeds, determined using a response surface design, were at a pH 9.0 and 1.3 M NaCl. Soy protein isolate (SPI) was included for comparison. Surface hydrophobicity of bitter melon seed protein isolate (BMSPI) (690) was significantly higher than that of SPI (399). Electrophoretograms of BMSPI showed bands at 40 and 55 kDa, and at 22, 25, and 35 kDa in non-reducing and reducing buffers, respectively. BMSPI had most of the essential amino acids and hence could be considered as a high quality protein. BMSPI had a single denaturation temperature (113.1 °C) while SPI had two denaturation temperatures (78.0 and 94.8 °C). The proteins exhibited U-shaped curves with solubilities ranging from 62.0% to 67.5% for BMSPI and 86.7% to 90.1% for SPI at pH ? 7.0. BMSPI had lower emulsifying activity (0.36 vs. 0.73), foaming capacity (39.6 vs. 61.0 ml), and foaming stability (21.5 vs. 25.5 min) than had SPI.     

Antimicrobial Activities of Phenolic Extracts Derived from Seed Coats of Selected Soybean Varieties

Soybean hulls or seed coats consist of complex carbohydrates, proteins, lipids, and polyphenols such as anthocyanidins, proanthocyanidins, and isoflavones. The polyphenolics in the seed coats give them various colors such as black, brown, green, yellow, or even a mottled appearance. In this study, the antimicrobial effects of phenolic extracts from the seed coats of different colored soybeans (yellow, dark brown, brown, and black) were evaluated against foodborne pathogens such as Salmonella Typhimurium, Escherichia coli O157:H7, and Campylobacter jejuni in broth‐cultures as well as on chicken skin. The highest total phenolic content was observed for the phenolic extract from soybean variety (R07‐1927) with black colored seed coat (74.1 ± 2.1 mg chlorogenic acid equivalent [CAE]/g extract) and was significantly different (P <0.0001) from the extract of the conventional soybean variety (R08‐4004) with yellow colored seed coat (7.4 ± 1.2 mg CAE/g extract). The extract from black colored soybean produced reductions of 2.10 ± 0.08 to 2.20 ± 0.08‐log CFU/mL for both E. coli O157:H7 and C. jejuni after 3 d when incubated in broth‐culture having 4‐log CFU/mL of bacteria, whereas a 6 d incubation was found to reduce S. Typhimurium and E. coli O157:H7 at 2.03 ± 0.05 and 3.3 ± 0.08‐log CFU/mL, respectively. The extract also reduced S. Typhimurium and E. coli O157:H7 attached to chicken skin by 1.39 ± 0.03 and 1.24 ± 0.06‐log CFU/g, respectively, upon incubation for 6 d. Soybean seed coat extracts may have a potency as antimicrobial agents to reduce foodborne bacteria contaminating poultry products.     

Bioactivity of a Rice Bran–Derived Peptide and Its Sensory Evaluation and Storage Stability in Orange Juice

A pentapeptide prepared from rice bran demonstrated growth inhibition on human lung, liver, breast, and colon cancer cell lines. The objectives of this study were to evaluate the human prostate cancer growth inhibition by the pentapeptide and its 6‐mo storage stability by incorporating spray‐dried orange juice, and determining sensory acceptability. The pentapeptide showed inhibition of human prostate cancer cells by 45% at 460 μg/mL concentration. When incorporated in spray‐dried orange juice, and reconstituted with water and tested, there was an approximately 10% degradation of the peptide at 620 μg/mL concentration under refrigerated conditions over a 6 mo storage period, whereas at ambient temperature the degradation was 30%. Larger degradation was observed when 240 or 460 μg/mL pentapeptide was used. Overall, consumer panelists liked sensory aspect of the reconstituted pentapeptide incorporated orange juice beverage. Also consumer panelists liked the color and mouthfeel attributes, their hedonic impression of flavor attribute was slightly low due to unpalatable bitter note caused by the presence of the peptide. Incorporation of the pentapeptide in spray‐dried orange juice has the potential to serve as a functional food ingredient that can offer health benefits to consumers. It is possible that the structural instability can be minimized by encapsulation.     

Total Phenolic Contents and Phenolic Acid Constituents in 4 Varieties of Bitter Melons (Momordica charantia) and Antioxidant Activities of their Extracts

ABSTRACT: Four varieties of bitter melon ( Momordica charantia ), India green (IG), India white (IW), China green (CG), and China white (CW) were analyzed for total phenolics, phenolic acid constituents, and antioxidant activities of their methanolic extracts. Phenolic contents of the oven-dried and freeze-dried tissues ranged from 5.39 to 8.94 and 4.64 to 8.90 mg chlorogenic acid equivalent (CAE)/g on dry weight basis, respectively. Phenolic contents of bitter melon seed, inner tissues, and flesh ranged from 4.67 to 8.02, 4.64 to 8.94, and 5.36 to 8.90 mg CAE/g, respectively. The total phenolic contents of IG, IW, CG, and CW were 4.64 to 6.84, 6.03 to 8.94, 5.39 to 7.81, and 6.07 to 8.90 mg CAE/g, respectively. The main phenolic acids in flesh were gallic acid, gentisic acid, catechin, chlorogenic acid, and epicatechin, which ranged from 8.04 to 39.76, 16.99 to 32.39, 23.06 to 82.45, 4.55 to 15.83, and 16.14 to 44.28 mg/100 g on dry weight basis, respectively, while in inner tissues were gallic acid, gentisic acid, catechin, and epicatechin, which ranged from 2.57 to 18.05, 5.39 to 32.61, 13.54 to 39.74, and 2.96 to 40.91 mg/100 g, respectively. The main phenolic acids contained in seeds were gallic acid, catechin, and epicatechin, which ranged from 4.61 to 18.9, 13.2 to 57.61, and 6.00 to 40.08 mg/100 g, respectively. There was no significant difference in the antioxidant activities of the extracts among varieties ( P = 0.2556) and between drying methods ( P = 0.1444). The antioxidant activities of flesh, inner tissue, and seed ranged from 81.7% to 86.5%, 78.8% to 88.4%, and 78.5% to 85.4% inhibition, respectively. Bitter melon is a rich source of phenolic compounds. These natural plant phenolics can be a good source of antioxidants for application in food system.