Influence of degree of hydrolysis on functional properties,antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate

Functional properties, antioxidant and Angiotensin-converting enzyme (ACE) inhibitory activities of peanut protein isolate (PPI) and peanut protein hydrolysate (PPH) prepared using Alcalase, at different (10%, 20%, 30% and 40%) degrees of hydrolysis, (DH) were investigated. Hydrolysis (at DH > 10%) significantly (p < 0.05) improved the solubility (>80%) of PPI, especially in the pH range of 4–6. However, PPI showed better emulsifying and foaming properties than PPH (p < 0.05). As DH increased, ferrous ion chelating activity, 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging activity and ACE inhibitory activity of PPH increased, while reducing power decreased (p < 0.05). Bleaching of beta-carotene by linoleic acid was suppressed better by PPI and PPH at 10% DH than of PPH at higher DH. Thus, the results reveal that DH affects functional properties, antioxidant and ACE inhibitory activities of peanut protein.     

米糟蛋白酶解制备生物肽及其抗氧化活性的研究

为了高值化利用米糟资源,以米糟蛋白为原料通过酶解法生产一种高效、低毒的天然米糟抗氧化肽。实验结果表明:7种蛋白酶中,中性酶为最佳酶选,其最佳酶解条件为:米糟蛋白质量浓度(S)为10g/100mL,中性酶浓度(E/S,质量分数)为8%,pH为6.0,温度为60℃,时间为30min。在该最佳酶解条件下,米糟生物肽的得率为18.50%,水解度为2.84%,DPPH.(1,2-二苯代苦味肼基自由基)清除率为90.10%。该米糟生物肽具有较强的DPPH和羟自由基清除能力,其IC50值(抗氧化活性为50%时所对应的米糟生物肽质量浓度)分别为1.136、0.169g/L,还具有较强的还原能力和Fe2+螯合能力(IC50值为2.127g/L)。由此得出,米糟蛋白是一种很好的米糟抗氧化肽生产原料,且该生物肽是一种较为理想的天然抗氧化剂产品。     

蛋白组分对米蛋白功能性质影响的研究

以不同配比米蛋白组分的样品为试材,比较各样品的功能性质变化,明确各蛋白组分对蛋白产品品质影响的差异,为今后进行分子设计和重组生产米蛋白产品提供理论支撑。通过各蛋白样品的溶解性,乳化特性,起泡特性,持水性/持油性等功能性质研究,结果表明,米糠浓缩蛋白的溶解性比大米浓缩蛋白高200%左右;米糠蛋白各功能性质显著优于大米蛋白,但大米蛋白的起泡稳定性比米糠蛋白提高近20%。米蛋白中的清蛋白提高产品的溶解性、持水性/持油性,降低起泡稳定性;醇溶蛋白提高产品的乳化特性;谷蛋白提高产品的起泡稳定性。蛋白产品的功能性质与蛋白组分的组成密切相关。     

产米渣蛋白水解酶菌株的筛选及鉴定

筛选产米渣蛋白水解酶菌株以促进米渣的绿色开发及充分利用。采用酪蛋白平板法从富含蛋白的样品初筛到115株产蛋白酶菌株。初筛菌株以米渣为唯一碳、氮源经发酵培养,通过复筛以分析其所产的蛋白酶,从豆豉中获得一株产米渣蛋白水解酶的目标菌株HP60。该菌株的粗酶活和对米渣蛋白的水解度分别达(263±7)U/m L和15.63%±0.30%。通过形态学、生理生化特征(API 20 NE,Biolog GP)及16S r RNA序列分析,鉴定HP60为解淀粉芽孢杆菌(Bacillus amyloliquefaciens),并已保藏于中国典型培养物保藏中心,保藏编号:CCTCC NO.M 2014200。本研究筛选的Bacillus amyloliquefaciens HP60对米渣蛋白的微生物开发奠定了一定基础。      

酰化和酶水解对菜籽蛋白功能性质和抗氧化活性的影响

研究乙酰化和丁二酰化对菜籽蛋白功能性质和抗氧化活性的影响,以及碱性蛋白酶水解对酰化菜籽蛋白功能性质和抗氧化活性的影响。结果表明,乙酰化和丁二酰化能明显提高菜籽蛋白的水溶性、吸油性和乳化性,但对乳化稳定性和起泡性影响不大,泡沫稳定性略有增加;酰化反应还能提高菜籽蛋白对DPPH自由基的清除率;酶水解酰化菜籽蛋白能显著提高水溶性,同时提高乙酰化菜籽蛋白对DPPH自由基的清除率。     

Chemical,antioxidant, functional and thermal properties of rice bran proteins after yeast and natural fermentations

The paper focuses on the chemical, antioxidant, functional and thermal properties of rice bran proteins after yeast, natural fermentations and unfermented rice bran. Protein content of yeast‐fermented rice bran protein concentrate (YFRBPC), naturally fermented rice bran protein concentrate (NFRBPC) and unfermented rice protein concentrate (UFRBPC) were 72.50%, 68.92% and 65.73%, respectively, while ash content were 4.72%, 4.61% and 3.04%, respectively. The total amino acids of YFRBPC, NFRBPC and UFRBPC were 123.16, 118.45 and 99.39, respectively. DPPH radical inhibition of YFRBPC, NFRBPC and UFRBPC were 58.62%, 55.29% and 47.14%, respectively, while ferric reducing ability power were 0.73, 0.58 and 0.41 mmol TE per gram, respectively. The highest foam capacity of UFRBPC (57.56%), NFRBPC (64.15%) and YFRBPC (76.00%) was observed at pH 9.0. YFRBPC and NFRBPC were lighter in colour than UFRBPC. YFRBPC had higher denaturation temperature and enthalpy value than NFRBPC and UFRBPC. The β‐sheets structures were more in YFRBPC and NFRBPC than UNFBPC.     

Enzymatic hydrolysis of hemp (Cannabis sativa L.) protein isolate by various proteases and antioxidant properties of the resulting hydrolysates

Enzymatic hydrolysis of hemp protein isolate (HPI) by six proteases (alcalase, flavourzyme, neutrase, protamex, pepsin and trypsin) and antioxidant activities of the resulting hydrolysates, obtained for 2 and 4 h were investigated. The yield of trichloroacetic acid (TCA)-soluble peptides (Y_sp), protein composition and surface hydrophobicity (H_o) of the hydrolysates were evaluated. The results showed that the hydrolysates exhibited varying DPPH radical scavenging (with lowest IC₅₀, ∼2.3 mg/mL) and Fe²⁺⁺ chelating (with lowest IC₅₀ of 1.6–1.7 mg/mL) abilities and reducing power (with highest absorbance at 700 nm of 0.31–0.35), depending on their Y_sp and H_o values. The DPPH radical scavenging and Fe²⁺⁺ chelating abilities of the hydrolysates were positively correlated with their Y_sp or H_o values. The results suggest that enzymatic hydrolysis can be used as an effective technique to produce high value-added products of hemp proteins.     

Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis

Antioxidant activity and functional properties of porcine blood plasma protein hydrolysates (PPH) prepared with Alcalase at 6.2%, 12.7% and 17.6% of degree of hydrolysis (DH) were investigated. The PPH showed stronger radical-scavenging ability and possessed stronger Cu²⁺-chelation ability and a reducing power compared to non-hydrolysed plasma protein (P < 0.05). The antioxidant activity of PPH, indicated by thiobarbituric acid-reactive substance (TBARS) values in a liposome-oxidising system, increased with increasing DH (P < 0.05). The Alcalase hydrolysis increased protein solubility from its original 68.46–81.79% (non-hydrolysed) to 82.95–94.94% (hydrolysed) over a broad pH range (3.0–8.0). However, hydrolysis decreased surface hydrophobicity and suppressed emulsifying and foaming capacity of the plasma protein. To identify antioxidant peptide, PPH was subjected to ultrafiltration, ion-exchange chromatography and reverse-phase high performance liquid chromatography (RP-HPLC), and the amino acid sequences of isolated peptides were determined by liquid chromatography/tendem mass spectrometry (LC–MS/MS). The peptide with the strongest antioxidant activity had the amino acid sequence of His-Asn-Gly-Asn. The results indicated that PPH could be used as a novel antioxidant but may be of limited utility as an emulsifying or foaming agent.     

Fish protein hydrolysates: Proximate composition,amino acid composition,antioxidant activities and applications: A review

The fish processing industry produces more than 60% by-products as waste, which includes skin, head, viscera, trimmings, liver, frames, bones, and roes. These by-product wastes contain good amount of protein rich material that are normally processed into low market-value products, such as animal feed, fish meal and fertilizer. In view of utilizing these fish industry wastes, and for increasing the value to several underutilised fish species, protein hydrolysates from fish proteins are being prepared by several researchers all over the world. Fish protein hydrolysates are breakdown products of enzymatic conversion of fish proteins into smaller peptides, which normally contain 2–20 amino acids. In recent years, fish protein hydrolysates have attracted much attention of food biotechnologists due to the availability of large quantities of raw material for the process, and presence of high protein content with good amino acid balance and bioactive peptides (antioxidant, antihypertensive, immunomodulatory and antimicrobial peptides).     

Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate

The effects of limited enzymatic hydrolysis by Alcalase on the conformational and functional properties of peanut (Arachis hypogaea L.) protein isolate (PPI) were investigated. Acid subunits of arachin were most susceptible to Alcalase hydrolysis, followed by conarachin and the basic subunits of arachin. Enzymatic hydrolysis increased the thermal stability of arachin and led to a sharp increase in the number of disulphide bonds with a decrease of the sulphydryl group in PPI hydrolysates in comparison with PPI. The analysis of intrinsic fluorescence spectra indicated a more moveable tertiary conformation of PPI hydrolysates than PPI. The limited emzymatic hydrolysis improved the functional properties of PPI, such as protein solubility and gel-forming ability, but impaired the emulsifying activity index.     

菜籽蛋白功能性质及抗氧化的研究进展

菜籽蛋白是一种完全蛋白,其营养价值高,总体品质优于大豆蛋白,甚至与动物蛋白或酪蛋白不相上下。菜籽蛋白不仅具有良好的功能性质如溶解性、乳化性、起泡性和凝胶性等,还具有良好的抗氧化活性,在食品工业和医药领域有很好的应用前景。但国内对于菜籽蛋白功能性质的研究相对较少,多集中在蛋白回收率的提高以及对有毒成分硫苷、植酸、多酚等的脱除。通过综述菜籽蛋白功能性质和抗氧化活性的研究进展,为今后菜籽蛋白的应用研究提供参考。     

糙米酵素乳饮料的功能成分及其抗氧化活性研究

将发芽糙米粉制成糙米酵素,经过一系列工艺制成风味独特的糙米酵素乳饮料。对其功能成分进行分析后并对其抗氧化活性进行研究。结果表明:糙米酵素乳饮料中的γ-氨基丁酸含量为0.225 mg/L,谷胱甘肽含量为48.9 mg/kg。其抗氧化性研究表明当质量浓度为1.0 mg/mL时,糙米酵素乳饮料对DPPH·的清除率高达83%,对超氧阴离子(O^2-·)的清除率为48%。     

还原糖对牡蛎蛋白肽糖基化反应产物功能特性与抗氧化性的影响

以葡萄糖(Glc)、乳糖(Lac)、半乳糖(Gal)为糖基供体,对牡蛎蛋白多肽(OP)进行干法糖基化改性,比较分析糖基化产物(OP-GMPs)的功能特性(溶解性、热稳定性和乳化性)及抗氧化性(还原能力,DPPH·、·OH的清除能力)。结果表明,与双糖(Lac)相比,单糖(Glc、Gal)对OP的功能特性和抗氧化性改善效果较好;其中,质量比Gal:OP=2:1时,OP-GMPs的溶解性最大且对DPPH·的清除能力最强,为3:1时,其乳化性最强,为4:1时,其对·OH的清除能力最强;Glc:OP=3:1和4:1时,OP-GMPs的热稳定性和还原能力最强。因此,糖基化改性可有效改善OP的功能特性与抗氧化活性,为其在功能食品及调味品中的应用提供参考。     

酶法水解脱脂米糠蛋白抗氧化性质研究

以脱脂米糠为原料,采用碱性蛋白酶、酸性蛋白酶和中性蛋白酶酶解制备米糠蛋白,并将制备酶解液与抗坏血酸在超氧阴离子自由基(O2-.)清除率、羟自由基(.OH)清除率、H2O2清除能力及还原能力等方面进行比较,研究米糠蛋白抗氧化活性。结果表明,米糠蛋白具有较强抗氧化活性,虽效果不如抗坏血酸;但对超氧阴离子自由基(O2-.)(最高为98.41%)、羟自由基(.OH)(最高达97.04%)及H2O2均有不同程度清除作用,并具有一定还原能力;且抗氧化能力与添加量存在一定量效关系,其中还出现有促氧化特殊现象。     

米糠蛋白的分离及其营养特性的研究

米糠中含有较高的蛋白质，其必需氨基酸组成近似于人体需要量模式，本文基于此原因，主要介绍了米糠蛋白的分离方法以及营养特性，相信米糠蛋白将成为食品工业的一种新型蛋白质。     

Rice Dreg Protein as an Alternative to Soy Protein Isolate: Comparison of Nutritional Properties

Rice dreg protein could be a valuable source of plant-based proteins, as an alternative to soy proteins in some food products. Here, nutritional properties of rice dreg protein were compared with those of soy protein isolate. The protein content of rice dreg protein was approximately 62.6 g/100 g sample, with large amounts of fat, carbohydrate, and ash. The denaturation temperatures of rice protein isolate from rice dreg protein were 47.4 and 97.2°C, respectively. This indicated that these proteins could be denatured during rice syrup processing to form aggregates, but were relatively more stable than rice endosperm protein and soy protein isolate. The main amino acids in rice dreg protein and rice protein isolate were Glu, Pro, Arg, Asp, and Leu, with Lys as the lowest content. Most of essential amino acids and nutritional parameters of rice protein isolate and rice dreg protein met the suggested nutritional requirements for a child according to FAO/WHO, and were relatively higher than those of soy protein isolate. In addition, rice protein isolate showed better digestibility than soy protein isolate during four hours sequential pepsin and pancreatin digestions. The final digestibility value was 96.66% for rice protein isolate compared to 91.41% for soy protein isolate. Thus rice dreg protein could potentially replace soy proteins as a good source of value-added protein for human nutrition in response to the increasing demand for plant proteins.     

Antioxidant activities and functional properties of soy protein isolate hydrolysates obtained using microbial proteases

Soy protein isolate (SPI) hydrolysates were prepared using microbial proteases to produce peptides with antioxidant activity. The process parameters (substrate and enzyme concentrations), hydrolysis time, functional properties and the effects of ultrafiltration were further investigated. The results showed that the soy protein isolate exhibited a 7.0‐fold increase in antioxidant activity after hydrolysis. The hydrolysis parameters, defined by the experimental design, were a substrate concentration of 90 mg mL^?1 and the addition of 70.0 U of protease per mL of reaction. The maximum antioxidant activities were observed between 120 and 180 min of hydrolysis, where the degree of hydrolysis was approximately 20.0%. The hydrolysis increased solubility of the soy protein isolate; however, the hydrolysates exhibited a tendency to decrease in the interfacial activities and the heat stability. The SPI hydrolysates fractions obtained by ultrafiltration showed that the enzymatic hydrolysis resulted in samples with homogenous size and strong antioxidant activity.     

酶法水解麦胚蛋白及其产物的抗氧化活性研究

选择碱性蛋白酶、中性蛋白酶、胰酶、木瓜蛋白酶和风味蛋白酶5种蛋白酶对麦胚蛋白进行水解,并考察其水解产物的抗氧化活性。结果表明,中性蛋白酶为制备麦胚抗氧化肽的最适蛋白酶,其最佳水解条件为:底物质量分数4%,酶添加量6 000U/g,酶解温度50℃,pH值7.5,水解至270min时抗氧化活性最大。     

Effects of three biological thiols on antimutagenic and antioxidant enzyme activities

The antimutagenic and antioxidant enzyme activities of captopril (CAP), cysteine (CYS), and glutathione (GSH) were evaluated for finding concentration-dependent inhibitory effects against: (1) the mutagenicity of 2-amino-3-methylimidazo [4,5-f] quinoline (IQ), an indirect mutagen; and (2) N-methyl-N′-nitrosoguanidine (MNNG), a direct mutagen toward Salmonellatyphimurium TA98 and TA100. Of the three thiols, CYS and GSH exhibited better inhibitory effects against IQ-induced mutation toward TA98 and TA100, respectively. GSH also showed a protective effect against MNNG-induced mutation toward TA98 and TA100, meanwhile, CAP showed the least inhibitory effect. CYS, GSH, and CAP also dose-dependently increased the activities of glutathione transferase, glutathione peroxidase, and glutathione reductase in hepatic BNL cells. CAP showed the superior inducing effects on glutathione transferase activity. These data suggested that the bioactive properties of biological thiols might contribute to their effects of antimutagenic activities as well as regulation on activities of antioxidant enzymes.     

Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type

Antioxidative activity and functional properties of protein hydrolysates from yellow stripe trevally (Selaroides leptolepis) meat, hydrolyzed by Alcalase 2.4L (HA) and Flavourzyme 500L (HF) with different degrees of hydrolysis (DH) were investigated. As the DH increased, DPPH radical-scavenging activity and reducing power of HA decreased (p < 0.05) but no differences were observed for HF (p > 0.05). Metal chelating activity of both HA and HF increased with increasing DH (p < 0.05). HF generally had a higher (p < 0.05) chelating activity than had HA at the same DH tested. At low DH (5%), HA exhibited a better DPPH radical-scavenging activity while, at high DH (25%), HF had a higher (p < 0.05) reducing power. For the functional properties, hydrolysis by both enzymes increased protein solubility to above 85% over a wide pH range (2–12). When the DH increased, the interfacial activities (emulsion activity index, emulsion stability index, foaming capacity, foam stability) of hydrolysates decreased (p < 0.05), possibly caused by the shorter peptide chain length. At the same DH, the functionalities of protein hydrolysate depended on the enzyme used. The results reveal that antioxidative activity and functionalities of protein hydrolysates from yellow stripe trevally meat were determined by the DH and by the enzyme type employed.