菌酶协同处理棉籽粕的营养特性、棉籽肽的制备及其抗氧化活性研究
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摘要
棉籽粕是世界范围内重要的植物蛋白原料,由于其含有棉酚等抗营养物质,蛋白消化利用率低等原因,限制了其在饲料中的大规模应用。近年来,已开发出以固态发酵为主的棉籽粕脱毒工艺,但对提高其蛋白品质,特别是涉及发酵后所产生的低分子量肽类的功能活性研究相对较少。鉴于此,本研究首先从实验室保藏的菌株中筛选出适合棉籽粕固态发酵的芽孢杆菌菌株,在此基础上,尝试筛选功能蛋白酶作为发酵佐剂进一步提高微生物发酵棉籽粕的效果；随后从棉籽粕中制备了棉籽肽组分并初步分析了其体外抗氧化活性和经过体外模拟消化后的稳定性；并进一步分离、纯化和鉴定了棉籽肽混合物中的单一抗氧化肽序列；最后通过双氧水诱导的小鼠巨噬细胞(RAW264.7)模型和Sprague-Dawley (SD)大鼠饲养试验,分别探讨了抗氧化棉籽肽对氧化损伤细胞的保护作用机制及其在动物体内的抗氧化效果。主要研究结果如下：
1.菌酶协同处理提高棉籽粕的营养品质
本试验以游离棉酚降解率和蛋白水解度为指标,对实验室保藏的7株芽孢杆菌进行筛选,并对接种量、发酵时间和发酵温度等发酵条件进行了响应面优化。在此基础上,从酸性蛋白酶、中性蛋白酶、碱性蛋白酶、风味蛋白酶和木瓜蛋白酶等5种蛋白酶中筛选合适的蛋白酶作为发酵佐剂用于棉籽粕发酵；并对菌酶协同处理后,棉籽粕的饲料常规营养成分、蛋白降解情况、体外消化率和抗氧化活性等进行分析。结果表明：(1)7株候选菌株中,枯草芽孢杆菌BJ-1可降低(p＜0.05)棉籽粕中的游离棉酚含量,同时提高(p＜0.05)其蛋白水解度,为合适的发酵菌株；(2)优化后芽孢杆菌BJ-1发酵棉籽粕的最佳条件为：接种量2%、发酵时间48h、发酵温度37℃,在此条件下,棉籽粕的脱毒率可达66.74%；(3)添加0.1%(w/v),即10000U/kg木瓜蛋白酶可进一步提高(p＜0.05)蛋白水解度,但对游离棉酚含量的影响不显著(p＞0.05)；(4)在采用木瓜蛋白酶和芽孢杆菌BJ-1协同处理棉籽粕后,与处理前相比,可提高(p＜0.05)其粗蛋白质和氨基酸含量,同时降低(p＜0.05)粗纤维、粗脂肪和游离棉酚含量；(5)菌酶协同处理棉籽粕还有效降解了棉籽蛋白的9s和5S组分,提高了(p＜0.05)棉籽蛋白的体外消化率和对1,1-二苯基苦基苯肼自由基(DPPH)的清除活性。结果提示,采用芽孢杆菌BJ-1发酵结合木瓜蛋白酶处理的方式可有效改善棉籽粕的营养品质。
2.棉籽肽的制备及其抗氧化特性研究
为了进一步分析菌酶处理对棉籽粕抗氧化活性的影响,试验从棉籽粕处理样品中提取了小于3kDa的低分子量肽类组分,确定了其化学组成和分子量分布,并以DPPH清除率、羟自由基清除率、金属离子螯合力和总还原力等为指标,对所提取棉籽肽的体外抗氧化活性进行了探讨。同时,采用胃蛋白酶和胰酶相结合的两步体外消化手段,分析了棉籽肽在模拟肠胃液消化后的蛋白降解情况、分子量分布改变和抗氧化功能。结果表明：(1)棉籽肽的体外抗氧化活性与其使用量和菌酶协同处理棉籽粕的时间均有关。在菌酶处理48h后,所提取棉籽肽的DPPH自由基、羟自由基清除活性,金属离子螯合能力和总还原力的半数效应浓度均达到最低值,分别为2.15、2.93、2.06和2.18mg/mL;(2)棉籽肽的氨基酸组成和分子量分布测定表明,其含有较多的谷氨酸、天冬氨酸和精氨酸,且疏水性氨基酸总量达到28.31%；同时分子量小于1kDa的组分占棉籽肽混合物的56.52%；(3)在采用胃蛋白酶和胰酶体外消化棉籽肽4h后,其蛋白水解度显著提高(p<0.05),肽段分子量进一步降低；(4)抗氧化活性分析表明,与消化前相比,棉籽肽的DPPH自由基清除率降低了40.3%(p＜0.05),羟自由基提高了36.64%(p＜0.05),金属离子螯合活力提高了17.62%(p＜0.05),总还原力降低了7.69%(p＜0.05)。结果提示,菌酶处理棉籽粕中提取的棉籽肽具有较高的体外抗氧化活性,为一种天然的抗氧化剂,且经过体外模拟消化后仍具有抗氧化功能。
3.抗氧化棉籽肽的分离纯化与结构鉴定
为了分析棉籽混合肽中的活性肽序列,通过将凝胶过滤色谱和制备型高效液相色谱相结合的方式对棉籽肽混合物中具有最高抗氧化活性的肽段进行分离纯化,并运用基质辅助激光解析电离飞行时间串联质谱对分离纯化得到的棉籽抗氧化肽的氨基酸序列进行解析。结果表明：(1)利用葡聚糖G-15凝胶色谱可将棉籽肽分成4个组分(A-D)；通过体外抗氧化活性分析发现,组分A具有最高的抗氧化活性；(2)制备型高效液相色谱可进一步将组分A分为9个主要组分(A-1-A-9),以DPPH自由基清除率为指标,筛选获得最强抗氧化肽组分A-8和A-9,并经分析型液相色谱鉴定为单一峰；(3)采用飞行时间串联质谱分析后,鉴定抗氧化肽A-8的相对分子量为823.37Da,氨基酸序列为STFAPSGSA;抗氧化肽A-9的相对分子质量为1752.78Da,氨基酸序列为GAAANDRDNPVRDDGPGG。
4.棉籽肽对小鼠巨噬细胞RAW264.7和SD大鼠抗氧化功能的影响
为了进一步探讨棉籽肽及其纯化组分A-8对氧化损伤细胞的保护作用及其可能机制,通过向小鼠巨噬细胞RAW264.7培养液中加入终浓度为600μM的双氧水诱导其产生氧化应激,并研究了棉籽肽及其纯化肽组分A-8(STFAPSGSA)对氧化损伤RAW264.7细胞活性、细胞基因组DNA、胞内抗氧化酶活、抗氧化代谢产物和细胞凋亡相关的p53基因表达的影响。另一方面,为了研究棉籽肽在动物机体内的抗氧化功能,将18只雄性SD大鼠(108.47±5.42g)随机分成3组,其中对照组大鼠饲喂基础日粮并灌喂生理盐水(1mL/d)；高脂组和棉籽肽处理组大鼠饲喂高脂日粮并分别灌喂1mL/d的生理盐水或浓度为2%的棉籽肽。试验结束后(14d),分别测定SD大鼠的增重情况、器官指数和血清及肝脏中的抗氧化酶活。结果表明：(1)棉籽肽对细胞基因组DNA的体外氧化损伤具有保护作用；(2)采用浓度为0.5和2.0mg/mL的棉籽肽或50μg/mL的纯化肽组分A-8预培养细胞12h,可降低(p＜0.05)双氧水对RAW264.7细胞活性的抑制作用；(3)与氧化应激组相比,添加2.0mg/mL的棉籽混合肽和50μg/mL的纯化肽组分A-8提高了(p＜0.05)细胞内的过氧化氢酶活性；棉籽混合肽及其组分A-8均可提高(p＜0.05)细胞内超氧化物歧化酶活性；浓度为0.5和2.0mg/mL的棉籽肽和50μg/mL肽组分A-8预处理细胞可提高(p＜0.05)细胞内谷胱甘肽过氧化物酶(GSH-Px)活性；(4)添加0.5mg/mL棉籽肽和50μg/mL的组分A-8均可降低(p＜0.05)细胞内的丙二醛(MDA)水平；(5)加入0.5或2.0mg/mL棉籽肽、50μg/mL的纯化组分A-8可降低(p＜0.05)细胞内凋亡基因p53的表达量；(6)体内试验表明,大鼠灌喂2%棉籽肽可提高(p＜0.05)其血清和肝脏中GSH-Px的活性,同时降低(p<0.05)血清中MDA和一氧化氮(NO)含量。以上结果提示,棉籽肽可在细胞水平和体内发挥抗氧化效果,其作用可能与相关抗氧化酶活性提高有关。
Cottonseed meal (CSM) is the world's leading plant protein resource. However, the application of CSM in feed industry is limited due to the gossypol and other anti-nutrients, as well as a relatively low protein digestibility. Recently, several detoxification procedures have been developed including the solid-state fermentation. However, studies for improving the protein quality of CSM are still scarce, particularly those involving the evaluation of functional properties of the cottonseed peptides (CPs). In the present study, a Bacillus subtilis strain was screened out for the solid-state fermentation of CSM. Then, one protease was selected as fermentation adjuvant to further improve the quality of CSM. The CPs were extracted from treated-CSM and its antioxidant activity was evaluated in vitro. The stability of CPs was accessed after a simulated gastrointestinal digestion. Then, two antioxidant peptides from CPs were successfully isolated, purified and their amino acid sequences were identified. Furthermore, the protective effects of CPs against hydrogen peroxide (H2O2)-induced oxidative damage in murine macrophages (RAW264.7), as well as the effects on oxidative status of cholesterol-fed rats were accessed. The findings are as follows:
1. Improvement of the nutritional quality of CSM by Bacillus subtilis and the addition of papain
Based on the results of free gossypol detoxification and degree of protein hydrolysis, seven Bacillus stains from our laboratory were screened. The fermentation conditions including the inoculum size, fermentation time and temperature were optimized using the response surface method. Five different kinds of proteases including the acid protease, neutral protease, alkaline protease, flavor protease and papain were also screened for CSM fermentation. The nutrient composition, protein degradation, in vitro digestibility and antioxidant activity of CSM treated with Bacillus and papain were determined. The results showed that:(1) B. subtilis BJ-1 could reduce (p<0.05) the free gossypol content and improve (p<0.05) the degree of protein hydrolysis (DH) among the seven candidate strains.(2) The optimal fermentation conditions by B. subtilis BJ-1were as follows:inoculum size2%, fermentation time48h, and fermentation temperature of37℃. Under these conditions, the detoxification rate of free gossypol was up to66.74%.(3) The addition of0.1%(w/v) papain further increased (p<0.05) the DH, but had no significant effect on the content of free gossypol.(4) Compared with the untreated meal, the contents of crude protein and amino acids increased (p<0.05) in CSM treated with B. subtilis BJ-1and papain, whereas the amount of crude fiber, crude fat and free gossypol were decreased (p<0.05).(5) Co-treatment by bacteria and enzyme also effectively degraded the9S and5S subunits of cottonseed protein, increased (p<0.05) the in vitro protein digestibility and1,1-diphenyl-2-picryl hydrazine (DPPH) free radical scavenging activity. The results suggest that the B. subtilis BJ-1fermentation with papain supplementation may offer an effective strategy to improve the quality of CSM.
2. Preparation and antioxidant properties of CPs
To further access the influence of fermentation with papain addition on the antioxidant activity of CSM, the CPs with molecular weight below3kD were extracted from CSM samples after B, subtilis BJ-1fermentation with papain supplementation and its chemical composition and molecular weight distribution were determined. CPs were further detected for their in vitro antioxidant activity including DPPH radical scavenging activity, hydroxyl radical scavenging activity, metal chelating ability and reducing power. The protein degradation, molecular weight distribution and antioxidant function of CPs were also measured after a simulated gastrointestinal digestion. The results showed that:(1) the in vitro antioxidant activity of CPs was closely related to its dosage and the fermentation time of B. subtilis BJ-1. The lowest half effect concentrations of DPPH radical, hydroxyl radical scavenging activity, metal chelating ability and reducing power were2.15,2.93,2.06, and2.18mg/mL, respectively, after a48-h treatment.(2) Amino acid analysis showed that CPs contained a large amount of glutamic acid, aspartic acid and arginine. The total hydrophobic amino acids were up to28.31%. The components of molecular weight less than1kDa accounted for56.52%of the total protein content.(3) The simulated gastrointestinal digestion increased (p<0.05) the DH as well as further reduced molecular weight distribution of CPs.(4) In vitro digestion decreased (p<0.05) DPPH radical scavenging activity and total reducing power by40.3%and7.69%, respectively. However, the digestion increased (p<0.05) hydroxyl radicals scavenging activity and metal chelating ability by36.64%and17.62%, respectively. The results suggest that the CPs may be used as a natural antioxidant and its antioxidant activity could be maintained after the digestion with pepsin and pancreatin.
3. Purification and identification of antioxidant peptides in CPs
The antioxidant peptides in CPs were isolated, purified by gel filtration chromatography and preparative liquid chromatography. Their amino acid sequences were further identified by using the matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry (MALDI-TOF MS/MS). The results showed that (1) the CPs were fractionated into four fractions (A-D) by gel filtration on Sephadex G-15column.(2) After investigated by in vitro methods, the fraction A demonstrated the highest DPPH scavenging activity and it can be further divided into main components (A-1-A-9) by the preparative high performance liquid chromatography. The fractions with the strongest antioxidant activity were named A-8and A-9.(3) The amino acid sequence of peptide A-8is STFAPSGSA, with a molecular weight of823.37Da. The amino acid sequence of peptide A-9is GAAANDRDNPVRDDGPGG, with a relative molecular mass of1752.78Da.
4. Effects of CPs on the antioxidant function of RAW264.7cells and Sprague-Dawley (SD) rats
To determine the protective effect of CPs on oxidative damage RAW264.7cells and its possible mechanism, RAW264.7cell culture was added with H2O2to a final concentration of600μM to induce oxidative stress. The effects of CPs and its A-8fraction (STFAPSGSA) on the cell viability, genomic DNA protection, intracellular antioxidant enzyme activity, and p53gene expression were measured. On the other hand, in order to study the impact of CPs on oxidative status of cholesterol-fed rats,18male SD rats (108.47±5.42g) were divided into three groups. The control rats were fed a basal diet and orally administrated physiological saline (1mL/d). Rats in the high-fat group and CPs-treated group were fed high-fat diets and oral administrated saline or2%CPs (1mL/d). The experiment lasted for14d. The results showed that:(1) CPs and purified peptide A-8could protect cell genomic DNA from in vitro oxidant damadge.(2) Pre-cultured cells with0.5and2.0mg/mL of CPs or50μg/mL of A-8reduced (p<0.05) the inhibition of RAW264.7cell viability.(3)2.0mg/mL of CPs and50μg/mL A-8components improved (p<0.05) catalase activity and superoxide dismutase activity.0.5,2.0mg/mL of CPs and50μg/mL of A-8fraction increased (p<0.05) intracellular activity of glutathione peroxidase (GSH-Px).(4) CPs (0.5mg/mL) and50μg/mL of A-8component reduced (p<0.05) the level of malondialdehyde (MDA).(5) Additionally, adding0.5or2.0mg/mL of CPs and50μg/mL of A-8purified fraction decreased (p<0.05) the p53gene expression.(6) In vivo tests showed that rats treated with2%CPs (1mL/d) had an increased (p<0.05) GSH-Px activity in serum and liver, as well as a lower (p<0.05) MDA and NO content in serum. These results suggest that the CPs could improve the antioxidant functions in both RAW264.7cells and rats under oxidant stress, and the protection may be related to the increase of antioxidant enzymes.
1.菌酶协同处理提高棉籽粕的营养品质
本试验以游离棉酚降解率和蛋白水解度为指标,对实验室保藏的7株芽孢杆菌进行筛选,并对接种量、发酵时间和发酵温度等发酵条件进行了响应面优化。在此基础上,从酸性蛋白酶、中性蛋白酶、碱性蛋白酶、风味蛋白酶和木瓜蛋白酶等5种蛋白酶中筛选合适的蛋白酶作为发酵佐剂用于棉籽粕发酵；并对菌酶协同处理后,棉籽粕的饲料常规营养成分、蛋白降解情况、体外消化率和抗氧化活性等进行分析。结果表明：(1)7株候选菌株中,枯草芽孢杆菌BJ-1可降低(p＜0.05)棉籽粕中的游离棉酚含量,同时提高(p＜0.05)其蛋白水解度,为合适的发酵菌株；(2)优化后芽孢杆菌BJ-1发酵棉籽粕的最佳条件为：接种量2%、发酵时间48h、发酵温度37℃,在此条件下,棉籽粕的脱毒率可达66.74%；(3)添加0.1%(w/v),即10000U/kg木瓜蛋白酶可进一步提高(p＜0.05)蛋白水解度,但对游离棉酚含量的影响不显著(p＞0.05)；(4)在采用木瓜蛋白酶和芽孢杆菌BJ-1协同处理棉籽粕后,与处理前相比,可提高(p＜0.05)其粗蛋白质和氨基酸含量,同时降低(p＜0.05)粗纤维、粗脂肪和游离棉酚含量；(5)菌酶协同处理棉籽粕还有效降解了棉籽蛋白的9s和5S组分,提高了(p＜0.05)棉籽蛋白的体外消化率和对1,1-二苯基苦基苯肼自由基(DPPH)的清除活性。结果提示,采用芽孢杆菌BJ-1发酵结合木瓜蛋白酶处理的方式可有效改善棉籽粕的营养品质。
2.棉籽肽的制备及其抗氧化特性研究
为了进一步分析菌酶处理对棉籽粕抗氧化活性的影响,试验从棉籽粕处理样品中提取了小于3kDa的低分子量肽类组分,确定了其化学组成和分子量分布,并以DPPH清除率、羟自由基清除率、金属离子螯合力和总还原力等为指标,对所提取棉籽肽的体外抗氧化活性进行了探讨。同时,采用胃蛋白酶和胰酶相结合的两步体外消化手段,分析了棉籽肽在模拟肠胃液消化后的蛋白降解情况、分子量分布改变和抗氧化功能。结果表明：(1)棉籽肽的体外抗氧化活性与其使用量和菌酶协同处理棉籽粕的时间均有关。在菌酶处理48h后,所提取棉籽肽的DPPH自由基、羟自由基清除活性,金属离子螯合能力和总还原力的半数效应浓度均达到最低值,分别为2.15、2.93、2.06和2.18mg/mL;(2)棉籽肽的氨基酸组成和分子量分布测定表明,其含有较多的谷氨酸、天冬氨酸和精氨酸,且疏水性氨基酸总量达到28.31%；同时分子量小于1kDa的组分占棉籽肽混合物的56.52%；(3)在采用胃蛋白酶和胰酶体外消化棉籽肽4h后,其蛋白水解度显著提高(p<0.05),肽段分子量进一步降低；(4)抗氧化活性分析表明,与消化前相比,棉籽肽的DPPH自由基清除率降低了40.3%(p＜0.05),羟自由基提高了36.64%(p＜0.05),金属离子螯合活力提高了17.62%(p＜0.05),总还原力降低了7.69%(p＜0.05)。结果提示,菌酶处理棉籽粕中提取的棉籽肽具有较高的体外抗氧化活性,为一种天然的抗氧化剂,且经过体外模拟消化后仍具有抗氧化功能。
3.抗氧化棉籽肽的分离纯化与结构鉴定
为了分析棉籽混合肽中的活性肽序列,通过将凝胶过滤色谱和制备型高效液相色谱相结合的方式对棉籽肽混合物中具有最高抗氧化活性的肽段进行分离纯化,并运用基质辅助激光解析电离飞行时间串联质谱对分离纯化得到的棉籽抗氧化肽的氨基酸序列进行解析。结果表明：(1)利用葡聚糖G-15凝胶色谱可将棉籽肽分成4个组分(A-D)；通过体外抗氧化活性分析发现,组分A具有最高的抗氧化活性；(2)制备型高效液相色谱可进一步将组分A分为9个主要组分(A-1-A-9),以DPPH自由基清除率为指标,筛选获得最强抗氧化肽组分A-8和A-9,并经分析型液相色谱鉴定为单一峰；(3)采用飞行时间串联质谱分析后,鉴定抗氧化肽A-8的相对分子量为823.37Da,氨基酸序列为STFAPSGSA;抗氧化肽A-9的相对分子质量为1752.78Da,氨基酸序列为GAAANDRDNPVRDDGPGG。
4.棉籽肽对小鼠巨噬细胞RAW264.7和SD大鼠抗氧化功能的影响
为了进一步探讨棉籽肽及其纯化组分A-8对氧化损伤细胞的保护作用及其可能机制,通过向小鼠巨噬细胞RAW264.7培养液中加入终浓度为600μM的双氧水诱导其产生氧化应激,并研究了棉籽肽及其纯化肽组分A-8(STFAPSGSA)对氧化损伤RAW264.7细胞活性、细胞基因组DNA、胞内抗氧化酶活、抗氧化代谢产物和细胞凋亡相关的p53基因表达的影响。另一方面,为了研究棉籽肽在动物机体内的抗氧化功能,将18只雄性SD大鼠(108.47±5.42g)随机分成3组,其中对照组大鼠饲喂基础日粮并灌喂生理盐水(1mL/d)；高脂组和棉籽肽处理组大鼠饲喂高脂日粮并分别灌喂1mL/d的生理盐水或浓度为2%的棉籽肽。试验结束后(14d),分别测定SD大鼠的增重情况、器官指数和血清及肝脏中的抗氧化酶活。结果表明：(1)棉籽肽对细胞基因组DNA的体外氧化损伤具有保护作用；(2)采用浓度为0.5和2.0mg/mL的棉籽肽或50μg/mL的纯化肽组分A-8预培养细胞12h,可降低(p＜0.05)双氧水对RAW264.7细胞活性的抑制作用；(3)与氧化应激组相比,添加2.0mg/mL的棉籽混合肽和50μg/mL的纯化肽组分A-8提高了(p＜0.05)细胞内的过氧化氢酶活性；棉籽混合肽及其组分A-8均可提高(p＜0.05)细胞内超氧化物歧化酶活性；浓度为0.5和2.0mg/mL的棉籽肽和50μg/mL肽组分A-8预处理细胞可提高(p＜0.05)细胞内谷胱甘肽过氧化物酶(GSH-Px)活性；(4)添加0.5mg/mL棉籽肽和50μg/mL的组分A-8均可降低(p＜0.05)细胞内的丙二醛(MDA)水平；(5)加入0.5或2.0mg/mL棉籽肽、50μg/mL的纯化组分A-8可降低(p＜0.05)细胞内凋亡基因p53的表达量；(6)体内试验表明,大鼠灌喂2%棉籽肽可提高(p＜0.05)其血清和肝脏中GSH-Px的活性,同时降低(p<0.05)血清中MDA和一氧化氮(NO)含量。以上结果提示,棉籽肽可在细胞水平和体内发挥抗氧化效果,其作用可能与相关抗氧化酶活性提高有关。
Cottonseed meal (CSM) is the world's leading plant protein resource. However, the application of CSM in feed industry is limited due to the gossypol and other anti-nutrients, as well as a relatively low protein digestibility. Recently, several detoxification procedures have been developed including the solid-state fermentation. However, studies for improving the protein quality of CSM are still scarce, particularly those involving the evaluation of functional properties of the cottonseed peptides (CPs). In the present study, a Bacillus subtilis strain was screened out for the solid-state fermentation of CSM. Then, one protease was selected as fermentation adjuvant to further improve the quality of CSM. The CPs were extracted from treated-CSM and its antioxidant activity was evaluated in vitro. The stability of CPs was accessed after a simulated gastrointestinal digestion. Then, two antioxidant peptides from CPs were successfully isolated, purified and their amino acid sequences were identified. Furthermore, the protective effects of CPs against hydrogen peroxide (H2O2)-induced oxidative damage in murine macrophages (RAW264.7), as well as the effects on oxidative status of cholesterol-fed rats were accessed. The findings are as follows:
1. Improvement of the nutritional quality of CSM by Bacillus subtilis and the addition of papain
Based on the results of free gossypol detoxification and degree of protein hydrolysis, seven Bacillus stains from our laboratory were screened. The fermentation conditions including the inoculum size, fermentation time and temperature were optimized using the response surface method. Five different kinds of proteases including the acid protease, neutral protease, alkaline protease, flavor protease and papain were also screened for CSM fermentation. The nutrient composition, protein degradation, in vitro digestibility and antioxidant activity of CSM treated with Bacillus and papain were determined. The results showed that:(1) B. subtilis BJ-1 could reduce (p<0.05) the free gossypol content and improve (p<0.05) the degree of protein hydrolysis (DH) among the seven candidate strains.(2) The optimal fermentation conditions by B. subtilis BJ-1were as follows:inoculum size2%, fermentation time48h, and fermentation temperature of37℃. Under these conditions, the detoxification rate of free gossypol was up to66.74%.(3) The addition of0.1%(w/v) papain further increased (p<0.05) the DH, but had no significant effect on the content of free gossypol.(4) Compared with the untreated meal, the contents of crude protein and amino acids increased (p<0.05) in CSM treated with B. subtilis BJ-1and papain, whereas the amount of crude fiber, crude fat and free gossypol were decreased (p<0.05).(5) Co-treatment by bacteria and enzyme also effectively degraded the9S and5S subunits of cottonseed protein, increased (p<0.05) the in vitro protein digestibility and1,1-diphenyl-2-picryl hydrazine (DPPH) free radical scavenging activity. The results suggest that the B. subtilis BJ-1fermentation with papain supplementation may offer an effective strategy to improve the quality of CSM.
2. Preparation and antioxidant properties of CPs
To further access the influence of fermentation with papain addition on the antioxidant activity of CSM, the CPs with molecular weight below3kD were extracted from CSM samples after B, subtilis BJ-1fermentation with papain supplementation and its chemical composition and molecular weight distribution were determined. CPs were further detected for their in vitro antioxidant activity including DPPH radical scavenging activity, hydroxyl radical scavenging activity, metal chelating ability and reducing power. The protein degradation, molecular weight distribution and antioxidant function of CPs were also measured after a simulated gastrointestinal digestion. The results showed that:(1) the in vitro antioxidant activity of CPs was closely related to its dosage and the fermentation time of B. subtilis BJ-1. The lowest half effect concentrations of DPPH radical, hydroxyl radical scavenging activity, metal chelating ability and reducing power were2.15,2.93,2.06, and2.18mg/mL, respectively, after a48-h treatment.(2) Amino acid analysis showed that CPs contained a large amount of glutamic acid, aspartic acid and arginine. The total hydrophobic amino acids were up to28.31%. The components of molecular weight less than1kDa accounted for56.52%of the total protein content.(3) The simulated gastrointestinal digestion increased (p<0.05) the DH as well as further reduced molecular weight distribution of CPs.(4) In vitro digestion decreased (p<0.05) DPPH radical scavenging activity and total reducing power by40.3%and7.69%, respectively. However, the digestion increased (p<0.05) hydroxyl radicals scavenging activity and metal chelating ability by36.64%and17.62%, respectively. The results suggest that the CPs may be used as a natural antioxidant and its antioxidant activity could be maintained after the digestion with pepsin and pancreatin.
3. Purification and identification of antioxidant peptides in CPs
The antioxidant peptides in CPs were isolated, purified by gel filtration chromatography and preparative liquid chromatography. Their amino acid sequences were further identified by using the matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry (MALDI-TOF MS/MS). The results showed that (1) the CPs were fractionated into four fractions (A-D) by gel filtration on Sephadex G-15column.(2) After investigated by in vitro methods, the fraction A demonstrated the highest DPPH scavenging activity and it can be further divided into main components (A-1-A-9) by the preparative high performance liquid chromatography. The fractions with the strongest antioxidant activity were named A-8and A-9.(3) The amino acid sequence of peptide A-8is STFAPSGSA, with a molecular weight of823.37Da. The amino acid sequence of peptide A-9is GAAANDRDNPVRDDGPGG, with a relative molecular mass of1752.78Da.
4. Effects of CPs on the antioxidant function of RAW264.7cells and Sprague-Dawley (SD) rats
To determine the protective effect of CPs on oxidative damage RAW264.7cells and its possible mechanism, RAW264.7cell culture was added with H2O2to a final concentration of600μM to induce oxidative stress. The effects of CPs and its A-8fraction (STFAPSGSA) on the cell viability, genomic DNA protection, intracellular antioxidant enzyme activity, and p53gene expression were measured. On the other hand, in order to study the impact of CPs on oxidative status of cholesterol-fed rats,18male SD rats (108.47±5.42g) were divided into three groups. The control rats were fed a basal diet and orally administrated physiological saline (1mL/d). Rats in the high-fat group and CPs-treated group were fed high-fat diets and oral administrated saline or2%CPs (1mL/d). The experiment lasted for14d. The results showed that:(1) CPs and purified peptide A-8could protect cell genomic DNA from in vitro oxidant damadge.(2) Pre-cultured cells with0.5and2.0mg/mL of CPs or50μg/mL of A-8reduced (p<0.05) the inhibition of RAW264.7cell viability.(3)2.0mg/mL of CPs and50μg/mL A-8components improved (p<0.05) catalase activity and superoxide dismutase activity.0.5,2.0mg/mL of CPs and50μg/mL of A-8fraction increased (p<0.05) intracellular activity of glutathione peroxidase (GSH-Px).(4) CPs (0.5mg/mL) and50μg/mL of A-8component reduced (p<0.05) the level of malondialdehyde (MDA).(5) Additionally, adding0.5or2.0mg/mL of CPs and50μg/mL of A-8purified fraction decreased (p<0.05) the p53gene expression.(6) In vivo tests showed that rats treated with2%CPs (1mL/d) had an increased (p<0.05) GSH-Px activity in serum and liver, as well as a lower (p<0.05) MDA and NO content in serum. These results suggest that the CPs could improve the antioxidant functions in both RAW264.7cells and rats under oxidant stress, and the protection may be related to the increase of antioxidant enzymes.
引文
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