Structural and antioxidative properties of royal jelly protein by partial enzymatic hydrolysis

The objective of this study was to investigate the structural and antioxidative properties of royal jelly protein(RJP)at different degrees of hydrolysis(DH)by partial enzymatic hydrolysis. RJP was hydrolyzed by alcalase for 0 min, 15 min, 1 h, 5 h and 8 h to obtain hydrolysates at DH of 5.34%, 11.65%, 15.19%, 21.38% and 23.91%, respectively. With the increased DH, the RJP hydrolysates showed elevated antioxidative activities. The molecular weight of RJP hydrolysates was significantly decreased but their primary backbone kept unchanged. Analysis of circular dichroism spectra revealed that the enzymolysis reduced the content of α-helix but increased the contents of β-sheet, β-turn and random coil. Meanwhile, the surface hydrophobicity and fluorescence intensity of RJP hydrolysates were decreased and a red shift occurred. As the enzymolysis continued, the surface morphology of RJP was gradually changed from a sheet-like structure into microparticles. Changes in antioxidative activities and structures generally followed a DH-dependent manner, however these changes became insignificant for samples at DH beyond 20%. Taking into consideration of both effectiveness and productivity, the optimum enzymatic duration was determined at 5 h.

Antioxidant Activities of Okra Protein Concentrate and Isolate after Enzymatic Hydrolysis

Three different proteolytic enzymes (pepsin, trypsin and papain) were used to prepare okra seed protein concentrate and okra seed protein isolate hydrolysates. The hydrolysates were assayed for antioxidant properties using radical scavenging, reducing power and metal chelating assays. The highest degree of hydrolysis (after 360 min) for okra protein isolates was 35.20%, 35.21% and 10.53% for pepsin, papain and trypsin respectively. The highest degree of hydrolysis (after 360 min) for okra protein concentrates was 26.8%, 28.59% and 6.47% for pepsin, papain and trypsin respectively. Pepsin hydrolysates showed higher metal chelating activity and radical scavenging activity than trypsin and papain hydrolysates. Trypsin hydrolysates showed the lowest antioxidant activities, which may be due to the low degree of hydrolysis. In general, for antioxidant activity, there was an increase in activity with an increase in the degree of hydrolysis. Similar antioxidant activity was found in both the okra protein isolate and concentrate hydrolysates except for metal chelating activity which was higher in okra protein isolate hydrolysates. This may be due to the higher ash concentration in the concentrates (9.4% in concentrates vs. 2.6% in isolates). In this study, pepsin hydrolysates with a final DH of 35.2% showed higher reducing power and metal chelating activity than trypsin and papain hydrolysates. Okra protein hydrolysates were found to have varying levels of antioxidant activity, which was dependent on the specificity of the protease and proportional to the degree of hydrolysis achieved.

Techniques Optimization of Combined Enzymatic Hydrolysis on Brewers＇ Spent Grain from Novozymes

Purpose： To extract protein, decrease the cellulose and facilitate the digestion and absorption of brewers＇ spent grain by animal. Topic： Discuss and optimize the hydrolysis conditions of the combined enzymatic hydrolysis by Novozymes. Method： The fresh brewers＇ spent grain was firstly dried, smashed and sifted. Then as indicators of the protein extraction rate in the enzyme solution and the content of cellulose in the index, the parameters of enzymatic hydrolysis, such as the solid-liquid ratio, reaction temperature, pH, enzyme dosage and reaction time, were investigated in detailed. After hydrolysis, the brewers＇ spent grain was put in the boiling water bath for inactivation for 15 minutes, and centrifuged, the supernatants were volume to 100 mL and the protein content was measured. After the precipitate was dried, the cellulose content was also measured. Achievements： The optimized conditions were with temperature of 50 ℃, pH 6.5, enzyme amount of 30 mg for Novozymes enzyme and 2.5 h for reaction time. Under these conditions, the protein extraction rate in the enzyme reaction reached 41.82%, and the cellulose content reached 13.90%, the degradation rate of cellulose was 18.86%.

The Effect of Hydrolysis with Neutrase on Molecular Weight,Functional Properties,and Antioxidant Activities of Alaska Pollock Protein Isolate

In this study, the Alaska pollock protein isolate(APPI) was hydrolyzed by Neutrase for 20, 40, 80, 120, 160, 200, and 240 min. Hydrolysates with different molecular weights were produced and they were named as H1–H7. Furthermore, the effects of hydrolysis on the average molecular weights, functional properties(solubility, oil-holding capacities, foaming activities, and emulsifying properties), and antioxidant activities(1, 1-diphenyl-2-picrylhydrazyl, superoxide, and hydroxyl free radical-scavenging activities) were determined. It was found that when the degree of hydrolysis(DH) increased, the average molecular weights of the hydrolysates decreased significantly. The functional properties of APPI were also significantly improved. The hydrolysates of APPI exhibited better solubility, emulsifying activities, and foaming activities. Hydrolysates with low molecular weights(<1 kDa) had better solubility, oil-holding capacities, and emulsifying activities, while hydrolysates with higher molecular weights(>1 kDa) had better foaming activities. In addition, the hydrolysates exhibited excellent antioxidant properties, while the inhibition values of 1, 1-diphenyl-2-picryl hydroxyl(DPPH), superoxide, and hydroxyl free radical-scavenging activities, were 85.22%, 53.56%, and 75.00% respectively, when the concentration of the hydrolysates was 5.0 mg mL^(-1). The lower the average molecular weight was, the higher was the antioxidant activity. These results indicated that hydrolysis with Neutrase is an effective method for improving the functional and antioxidant properties of APPI. The hydrolysates of APPI displayed great potentials to be used as natural antioxidants in protein-rich aqueous foods such as nutrient supplements and sports beverages.

A Study of the Enzymatic Hydrolysis of Fish Frames Using Model Systems

A model system was employed to study the operating conditions and primary parameters of enzymic hydrolysis of cod proteins. Pancreatin, papain, and bromelain were used to hydrolyse minced cod fillets under controlled conditions and with the rate of hydrolysis being continually monitored via both the pH-stat and TNBS method. The two methods were compared and evaluated. The rate of protein solubilisation was plotted against the degree of hydrolysis (DH). Dry fish protein hydrolysate (FPH) powders having short, medium and high degrees of hydrolysis (DH of approximately 8%, 11% and 16% respectively) were produced and analysed for their molecular weight distribution, using size exclusion chromatography. Almost complete protein solubilisation (75 g soluble protein per kg hydrolysis solution) could be achieved within an hour, at 40oC, at 1% enzyme/substrate ratio (w/w) with papain and bromelain. The pH-stat was found capable of continuously following the rate of hydrolysis but only at low DH. The TNBS could be accurately used even at high DH to estimate the percentage of the peptide bonds cleaved, but required chemical analysis of withdrawn samples.

Dynamic changes of peptidome and release of polysaccharide in sea cucumber(Apostichopus japonicus) hydrolysates depending on enzymatic hydrolysis approaches

Enzymatic hydrolysis has been widely used to produce bioactive hydrolysates from sea cucumber body wall.Here,inspired by the clarification of Apostichopus japonicus genome,we investigated the enzymatic hydrolysis of sea cucumber body wall by using the omics strategy.Shared proteins,including major yolk proteins,collagens,extracellular matrix glycoproteins and muscle proteins,were released from the body wall by different hydrolysis condition.A portfolio of 216 shared peptides were detected in the peptidome by papain with different hydrolysis time,while 32 shared peptides were detected in the peptidome by differing proteases.Unshared peptides and the relative abundance distribution profiles of shared peptides changed depending on hydrolysis approaches,indicating dynamic changes of peptidome during hydrolysis.Moreover,release of sulfated fucan and fucosylated chondroitin sulfate changed with the hydrolysis condition.The monitoring of dynamic enzymatic hydrolysis process at a molecular scale would contribute to production and quality control of sea cucumber hydrolysates.

Isolation and Purification of Enzymatic Hydrolysates of Yam(Dioscorea opposita Thunb.)Proteins

Using yam （Dioscorea opposita Thunb. ） as the experimental material, enzymatic hydrolysates of yam proteins were prepared with alkaline protease, which were then isolated and purified by cellulose DE-52 anion exchange chromatography Sephadex G-50 gel chromatography. According to the results, four absorp- tion peaks were obtained by cellulose DE-52 anion exchange chromatography, and fractions at each absorption peak were collected. Specifically, the reducing ability of four peaks demonstrated a descending order of peak 2 （P2） 〉 peak I （ P1 ） 〉 peak 3 （P3） 〉 peak 4 （P4）. By Sephadex G-50 gel chmmatography, P1 and P2 were isolated and purified with distilled water and Tris-HC1 buffer, and two absorption peaks were obtained, respectively.

Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of <i>α</i>-Lactalbumin

Whey proteins are known for their high nutritional value and bioactivity, notably great potential is found on α-lactalbumin. The objective of this study was to evaluate antioxidant, antiglycant and ACE (angiotensin converting enzyme)-inhibitory activity of α-lactalbumin peptides obtained from enzymatic hydrolysis with Alcalase through different hydrolysis conditions. The optimization of enzymatic hydrolysis was studied by response surface methodology variating enzyme:substrate ratio (0.0050%, 0.0525% and 0.1000% w/w) and time (0, 30 and 60 minutes) measuring antioxidant activity by ABTS and ORAC-FL (response variables), founding an augment of this activity with time. Characterization of seven samples showed increasing hydrolysis with time. Hydrolysate obtained with 0.1000% w/w and 60 minutes demonstrated higher antioxidant activity related to greater hydrolysis. This hydrolysate did not show antiglycant activity but promoted advanced glycation end products formation with methylglyoxal and glucose. In contrast, this sample showed 30% of ACE inhibition when compared to Captopril, having great potential by enhancing hydrolysis.

羊乳清蛋白部分和深度水解工艺、水解物致敏性及肽谱分析

利用羊乳清蛋白制备低致敏性配料是目前乳品工业的研究热点。乳清蛋白是乳中主要的蛋白质之一,也是引起婴幼儿过敏反应的主要成分,将蛋白质水解为小分子肽是降低其致敏性的有效方法。以山羊乳清蛋白为原料,研究了部分水解乳清蛋白和深度水解乳清蛋白的水解工艺和水解物特性(水解度、分子质量分布和β-乳球蛋白抗原性),并利用液相色谱串联质谱法(L C-MS/MS)比较了部分水解和深度水解工艺中过敏表位酶切位点的差异。研究结果表明,中性蛋白酶和碱性蛋白酶对羊乳清蛋白水解效果较好,其中碱性蛋白酶的水解度最高,达21.26%。经电泳分析,单酶水解后的产物中仍存在大分子多肽链,深度水解工艺需要复合酶水解。在酶底比为4000 U/g时,使用碱性蛋白酶在pH值为10.0、温度为55℃条件下水解羊乳清蛋白1.0 h,部分水解产物的水解度为12.31%,分子质量在5 kDa以下的多肽占95.18%,β-乳球蛋白抗原性下降率为9.40%。中性蛋白酶和碱性蛋白酶的质量比为1∶1,酶底比为6000 U/g,在pH值为8.5、温度为50℃条件下,水解羊乳清蛋白3.0 h,深度水解产物的水解度为35.58%,分子质量低于3 kDa的多肽为97.26%,β-乳球蛋白抗原性下降率为40.97%。部分水解和深度水解均能破坏β-乳球蛋白的大部分过敏表位,但相较于部分水解,深度水解能更大程度地降低乳清蛋白的致敏性。研究旨在为低致敏性羊水解乳清蛋白的生产提供一定的理论参考。

超声辅助酶法提取玉米胚芽粕水解蛋白及其抗氧化活性

以玉米胚芽粕为原料,研究超声波辅助碱性蛋白酶提取玉米胚芽粕水解蛋白的工艺条件。通过单因素试验初步确定超声波辅助酶法提取玉米胚芽粕水解蛋白的条件,在单因素试验基础上进行正交试验设计,并测定其抗氧化活性。结果表明,最优提取条件为超声温度50℃、超声时间50 min、超声功率140 W,在此条件下,玉米胚芽粕的水解蛋白提取率为90.6%。对DPPH自由基和羟自由基的IC_(50)分别为17.56µg/mL和28.41µg/mL。

绿豆蛋白α-淀粉酶抑制肽的制备与鉴定

采用胃-胰蛋白酶水解绿豆蛋白及其分级蛋白,以水解物α-淀粉酶活性抑制率为主要指标,结合水解度、氨基酸组成及分子质量分析其抑制效果差异及原因。结果表明,绿豆蛋白肽对α-淀粉酶活性抑制率最高,为16.51%;与绿豆分级蛋白相比,绿豆蛋白的疏水氨基酸含量和水解度最高,分别为32.68%和6.28%,水解物的肽分子质量最小,均小于20kDa,因此选用绿豆蛋白制备α-淀粉酶抑制肽。然后分离鉴定绿豆蛋白肽,新发现了17条有潜在α-淀粉酶抑制效果的肽。本研究表明绿豆蛋白较其分级蛋白具有更强的α-淀粉酶抑制效果,能够用于降血糖的功能性食品或药物中。

发酵和酶解技术在猪蛋白原料开发中的应用研究

发酵和酶解技术是猪蛋白饲料原料开发中常用的生物处理手段,能显著提高饲料的营养价值,降低抗营养因子含量,并促进动物肠道消化吸收。尤其在蛋白饲料资源匮乏及非常规蛋白饲料资源利用率较低等背景下,发酵和酶解技术在猪蛋白原料开发中具有广阔的应用前景和潜力。文章主要阐述了发酵和酶解技术特点,总结了发酵、酶解及其协同处理原料的应用技术研究现状,并对发酵和酶解技术在应用中存在的问题和未来发展的方向进行了分析及展望。

莲子酶解动力学分析与酶解产物多糖的表征

为开发更温和与简便的高纯度植物多糖新型酶法水解提取工艺,该研究以胃蛋白酶(内肽酶)和曲蛋白酶(端肽酶)作为复合酶,建立酶解过程的动力学模型。对上述工艺所提取制备的多糖与45℃水提法、90℃水提法、胃蛋白酶提取法所制得的莲子多糖进行营养成分分析与结构(单糖组成、红外光谱、热特性、低场核磁和动态热机械)表征。构建单酶(胃蛋白酶)/双酶分段酶解的动力学模型;双酶法提取的莲子多糖中多酚浓度((0.42±0.008)mg/mL)和糖醛酸含量(15.65%±0.98%)最高,而以双酶法制得的莲子多糖蛋白质含量(0.73%±0.24%)最低;4种莲子多糖均含有葡萄糖(Glc)、阿拉伯糖(Arab)、甘露糖(Man)和鼠李糖(Rha),其中双酶法提取的多糖中半乳糖醛酸(Gal-UA)和Man的含量较多,分别为10.700%和10.752%;4种多糖均为α-型吡喃糖;双酶提取法相比水提法可有效降低莲子多糖中的蛋白质含量和玻璃化温度,提高结合水含量和亲水能力。酶解动力学模型可为莲子多糖纯化机制提供有效参考,尤其是双酶分段酶解法的特异性强、步骤简便,有利于提取和纯化莲子多糖成分,该研究可为动植物非淀粉类多糖的高质量提取和工业化生产提供理论基础。

酶解法制备阿胶蛋白肽工艺条件优化及抗氧化活性分析

目的:研究酶解法制备阿胶蛋白肽的工艺条件及阿胶蛋白肽的抗氧化活性。方法:以阿胶为原料,通过酶解实验优化碱性蛋白酶Alcalase 2.4L制备阿胶蛋白肽的酶解工艺条件。以酶解pH、酶与底物比、酶解温度作为考察因素,以阿胶的水解度为指标,在单因素实验的基础上,通过正交试验确定最佳工艺条件;利用高效凝胶色谱法测定酶解前后阿胶溶液的分子量分布情况,并通过检测对ABTS+和DPPH自由基的清除率,考察酶解前后阿胶溶液的抗氧化活性,从而综合分析酶解效果;采用4种不同大小孔径的超滤膜分离阿胶蛋白肽液,研究经超滤膜分离后不同分子量阿胶蛋白肽的抗氧化活性。结果:阿胶溶液的最佳酶解条件为:pH10.5、酶与底物比9%、酶解温度63℃,此条件下测得阿胶酶解液的水解度为15.93%±1.32%;酶解后阿胶溶液的分子量大部分分布在5000 Da以下;当浓度为10 mg/mL时,未酶解和酶解后的阿胶蛋白肽溶液ABTS+自由基清除率分别为75.83%±0.32%和93.16%±0.21%,DPPH自由基清除率为16.93%±2.41%和39.95%±1.27%;经超滤处理获得五组不同分子量的阿胶蛋白肽(>30 kDa、10~30 kDa、3~10 kDa、1~3 kDa和<1 kDa),分析比较发现低分子量的阿胶蛋白肽抗氧化效果较好。结论:碱性蛋白酶Alcalase 2.4L能够有效制备阿胶蛋白肽,且阿胶蛋白肽具有良好的抗氧化活性。试验结果为后续开展阿胶蛋白肽的抗氧化机制研究提供科学依据。

葛根蛋白酶解物大孔树脂吸附工艺优化及其体外抗氧化活性研究

目的:优化大孔树脂吸附葛根蛋白酶解物工艺及其抗氧化活性研究。方法:采用Box-Behnken响应面法确定大孔树脂吸附葛根蛋白酶解物最佳工艺。以维生素C为对照,测定最佳工艺下纯化前后葛根蛋白酶解物的抗氧化活性。结果:大孔树脂的最佳吸附—解吸工艺为上样液质量浓度10.0 mg/mL,洗脱液流速2.6 mL/min,洗脱液乙醇体积分数74%,纯化后葛根蛋白酶解物含量提升至37.19%。大孔树脂纯化后的葛根蛋白酶解物对DPPH自由基、ABTS+自由基、羟自由基的清除率均强于吸附前的。结论:大孔树脂纯化后的葛根蛋白酶解物抗氧化效果良好,可以作为一种潜在的蛋白多肽应用于食品中。

核桃粕源抗氧化活性肽的酶解制备及活性分析

目的:深度利用核桃粕蛋白。方法:采用分级分离法从核桃粕中提取蛋白质后,分别用胰蛋白酶、木瓜蛋白酶、中性蛋白酶、碱性蛋白酶和风味蛋白酶5种蛋白酶对其进行水解,并比较分析胰蛋白酶酶解物(trypsin hydrolysate,TH)、木瓜蛋白酶酶解物(papain hydrolysate,PH)、中性蛋白酶酶解物(dispase hydrolysate,DH)、碱性蛋白酶酶解物(alcalase hydrolysate,AH)和风味蛋白酶酶解物(flavourzyme hydrolysate,FPH)的抗氧化活性;以DPPH自由基清除率、ABTS自由基清除率和羟自由基清除率为检测指标分析不同浓度AH的体外抗氧化性;采用LC-MS/MS技术鉴定AH中所有肽的序列,并利用PeptideRanker、BIOPEP-UWM数据库和分子对接工具AutoDock1.5.6筛选潜在的核桃抗氧化活性肽;将上述两条肽分别与Keap1蛋白进行计算机模拟分子对接,并利用斑马鱼胚胎氧化损伤模型,对人工合成的两条抗氧化活性肽的抗氧化活性进行分析。结果:5种酶解物中抗氧化活性较好的AH对DPPH自由基、ABTS自由基和羟自由基的最佳清除率分别为(71.56±0.75)%,(60.63±0.45)%,(98.63±0.06)%。LC-MS/MS鉴定并通过计算机分析预测得到两条活性最优的肽,即:ALWPF和PLRWPF;两条抗氧化活性肽均能与Keap1蛋白的活性部位结合,其结合能分别为-9.2,-9.6 kJ/mol。ALWPF和PLRWPF肽处理斑马鱼胚胎的安全质量浓度范围分别为0~50,0~30μg/mL。结论:从核桃粕中鉴定出两条抗氧化肽,其对斑马鱼胚胎具有保护作用。

雪茄烟叶蛋白提取及其水解产物的氨基酸组成和抗氧化活性

【目的】研究雪茄烟叶蛋白提取及其水解产物的氨基酸组成和抗氧化活性,为烟叶蛋白资源的深度开发与利用提供理论依据和技术支撑。【方法】利用碱溶酸沉法提取雪茄烟叶蛋白,确定最佳提取条件;利用胃蛋白酶、复合蛋白酶、碱性蛋白酶、木瓜蛋白酶和中性蛋白酶对提取的蛋白进行水解,并对水解产物的氨基酸组成和抗氧化活性进行分析。【结果】雪茄烟叶蛋白的最佳提取条件为:料液比1∶25(g∶mL)、碱溶pH为8.0、碱溶时间80 min、提取温度60℃、酸沉pH为3.0,最佳提取率为79.08%。雪茄烟叶蛋白通过胃蛋白酶水解的效果最好,水解度为15.52%;其水解产物中游离氨基酸含量最高,必需氨基酸、疏水性氨基酸、负电荷氨基酸和正电荷氨基酸的含量也高于其他酶解产物,必需氨基酸与总氨基酸的比值、必需氨基酸与非必需氨基酸的比值均高于FAO/WHO标准规定值。随着水解时间的延长,水解产物对超氧阴离子自由基、DPPH自由基和羟自由基的清除能力呈上升趋势,且对超氧阴离子自由基的清除率最高(57.54%)。【结论】碱溶酸沉法能够较好地提取雪茄烟叶蛋白;通过胃蛋白酶水解雪茄烟叶蛋白,其氨基酸组成和比例得到改善,提升了营养价值,增强了其水解产物的抗氧化能力。

核桃仁原位水解工艺优化及氧化稳定性研究

为延长核桃仁货架期,提高核桃仁储藏品质。以去皮核桃仁为原料,利用复配蛋白酶(胰酶)酶解核桃仁实现原位富集抗氧化肽,采用单因素实验分别研究了底物质量分数、酶质量分数、水解温度、水解时间对水解液抗氧化活性的影响。在此基础上,采用正交实验确定最优水解工艺为:酶质量分数12%、底物质量分数40%、水解温度45℃、水解时间20 min。萃取酶解处理的核桃仁(样品组)和未处理的核桃仁(空白对照组)油脂测定其氧化诱导时间,将样品组和空白对照组用铝袋分装在60℃烘箱内加速氧化。结果表明,样品组具有更长的氧化诱导时间及Q10指数,其氧化自由能从59.896 kJ/mol上升到78.103 kJ/mol;加速氧化过程对照组过氧化值始终高于样品组,以过氧化值为指标结合油脂氧化规律得到在20℃下样品组货架期相对于对照组延长了68 d。

不同酶解路线大米蛋白肽的制备、表征及抗氧化活性

为探究双酶不同酶解路线制得大米蛋白肽的性质差异,研究采用胰蛋白酶(A)和碱性蛋白酶(B)按不同酶解路线对大米蛋白进行酶解,制备了5种大米蛋白肽(A^(1)B^(1)、A^(1)B^(2)、A^(2)B^(1)、A^(1*)B^(2)、A^(2)B^(1*)),对其水解度、基本成分、氨基酸组成、微观结构、二级结构、分子量分布、风味和体外抗氧化活性等进行分析。结果表明,A^(2)B^(1)组的蛋白含量最高达到90.69%,肽含量高达72.73%;各路线的水解度大于17.60%,水解较为完全;微观结构均由不规则块状变为球体状,A1B2组和A^(1*)B^(2)组球体壁较厚,A^(2)B^(1)组和A^(2)B^(1*)组球体壁较薄,A^(1)B^(1)组为球体碎片;各路线的必需氨基酸含量比大米蛋白低,A1B2组必需氨基酸含量最高;二级结构以多种构象并存,各路线二级结构均以β-转角为主,占二级结构的44.62%~47.18%;各路线酶解产物多为低分子量的多肽,分子量低于5 k Da的多肽占92.09%~93.71%;A1B2样品鲜味最强,涩味最弱,A^(2)B^(1)样品咸味和苦味最弱;相比于A^(1)B^(1)组、A1B2组和A^(1*)B^(2)组,A^(2)B^(1)组和A^(2)B^(1*)组的抗氧化活性更强。通过对双酶不同酶解路线大米蛋白肽的性质研究,综合基本成分、肽含量、氨基酸组成、风味和抗氧化活性评价,A^(2)B^(1)组的品质最佳。

超声辅助酶解制备大米蛋白黄嘌呤氧化酶活性抑制肽的工艺条件优化

以大米蛋白为原料,研究碱性蛋白酶酶解法制备黄嘌呤氧化酶(Xanthine Oxidase,XOD)活性抑制肽,并对其体外功能活性进行评价。研究了蛋白酶种类、底物质量分数、酶解温度、加酶量、酶解pH、酶解时间对大米蛋白水解度(degree of hydrolysis,DH)及酶解产物对黄嘌呤氧化酶活性抑制率的影响,探讨了不同超声处理方式对酶解过程的影响,通过响应面法对实验条件进行了优化结果为:采用碱性蛋白酶,底物质量分数5%,酶解温度为56℃,加酶量为8000 U/g,酶解pH为10,超声功率70 W,超声酶解60 min,对所制备的大米蛋白黄嘌呤氧化酶活性抑制肽的功能活性进行了评价。在最优条件下其黄嘌呤氧化酶抑制活性的IC_(50)为1.55 mg/mL,ABTS自由基清除作用、羟基自由基清除作用、DPPH自由基清除作用的IC_(50)值分别为0.49、12.48、3.88 mg/mL。