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Cui J Kong X Hua Y Zhou H Liu Q 《Journal of the science of food and agriculture》2011,91(15):2799-2805
BACKGROUND: The low solubility of wheat gluten is one of the major limitations to its use in food processing, and enzymatic hydrolysis has been found to be an effective way to prepare more soluble bioactive peptides from gluten. The aim of this study was to prepare bioactive peptides from modified wheat gluten (MWG) in a continuous enzymatic membrane reactor (EMR) that allowed rapid separation of low‐molecular‐weight peptides from hydrolysates, thus avoiding the disadvantages of batch reaction such as inefficient use of enzymes, inconsistent products due to batch‐to‐batch variation, substrate–product inhibition, low productivity and excessive hydrolysis. RESULTS: Wheat gluten was modified to decrease its lipid and starch contents in order to prevent membrane fouling. The optimal working conditions for Alcalase to hydrolyse MWG in the EMR were a substrate concentration of 20 g L?1, an enzyme/substrate ratio of 0.03, an operating pressure of 0.04 MPa, a temperature of 40 °C and a pH of 9. The operating stability of the EMR (including residual enzyme activity, productivity and capacity) was high. The permeate fractions showed antioxidant activities that were mostly due to low‐molecular‐weight peptides. A simple theoretical kinetic model was successfully applied to the enzymatic hydrolysis of MWG in the EMR. CONCLUSION: Modification of wheat gluten made the continuous enzymatic membrane reaction more efficient and the EMR proved to be an effective means of producing peptides with particular properties and bioactivities. The permeate fractions (mainly < 1000 Da) were homogeneous and stable and also showed strong antioxidant activities. Copyright © 2011 Society of Chemical Industry 相似文献
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酶解蛋白制备生物活性肽进展 总被引:11,自引:0,他引:11
该文主要对国内外制取活性肽的蛋白质资源、其酶解物功能特性、蛋白酶解工艺和活性肽制取 方法进行分析;由于活性肽独特生理功能,在保健食品和饲料工业有着广泛应用。 相似文献
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Panida Aiemratchanee Kulachatr Panyawechamontri Phutthaphorn Phaophu Onrapak Reamtong Watanalai Panbangred 《International Journal of Food Science & Technology》2021,56(5):2315-2324
New bioactive peptides with antihypertensive property from red blood corpuscle (RBC) and plasma (PL) hydrolysate fractions of porcine blood were identified. Three peptides with the highest Angiotensin-converting enzyme (ACE) inhibitory activity from RBC, including RBC7 (TPYPCV), RBC15 (VVYPWR) and RBC9 (FLCT), showed IC50 values of 2.58 ± 0.87, 5.22 ± 2.56 and 6.53 ± 0.34 µm , respectively. By comparison, PL1 (YTFPFH), PL2 (WGHGNPHV) and PL7 (VPLW) from PL displayed higher IC50 values at 24.12 ± 2.44, 15.33 ± 0.44 and 32.80 ± 38.96 µm , respectively. Molecular docking was employed to simulate the interactions of RBC7 and RBC15 with the catalytic site of the ACE receptor. RBC7 and RBC15 interacted with residues in the ACE receptor that normally coordinated with Zn(II), and RBC7 also interacted extensively with residues within S1, S2 and S’1 active sites. Taken together, these results illustrate that porcine blood is an excellent source of antihypertensive peptides and could be of great benefits to people with high blood pressure. 相似文献
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为了克服传统酶解技术的不足,提高酶解反应效率,采用不补料酶膜耦合反应制备牛乳蛋白ACE抑制肽。考察超滤膜对牛乳蛋白及酶的截留、膜通量及滤出液的ACE抑制率和IC50的影响,确定出超滤膜最佳的截留分子量为5000 u;研究了反应时间、底物浓度、加酶量和循环泵转速对蛋白转化率的影响,确定最优酶解工艺条件:底物浓度7%(W/W)、加酶量2000 U/g、反应时间100 min、循环泵转速100 r/min,该条件下蛋白转化率、单位酶产肽量、ACE抑制率分别达到53.16%、39.59 g肽/g酶、76.81%,与对照组相比蛋白转化率、单位酶产肽量、ACE抑制率分别提高了16.99%、16.61%、18.55%;采用高效凝胶过滤色谱法测定超滤液中ACE抑制肽的分子量分布,发现样品中分子量≤2253 u组分质量分数为94.62%,超滤膜对截留分子量大小控制准确。因此不补料酶膜耦合反应可为酶法制备牛乳蛋白ACE抑制肽提供一种更为高效的方法。 相似文献
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为研究蛋白酶酶解制备猪肠粘膜蛋白粉工艺,以天然猪肠衣加工副产物肠粘膜为原料,以酶解产物中可溶性蛋白含量为指标,通过单因素实验和响应面实验,筛选适宜用于酶解猪小肠粘膜的蛋白酶并对其酶解工艺条件进行优化。结果表明,木瓜蛋白酶酶解猪肠粘膜制备蛋白粉可溶性蛋白含量达7.37%±0.06%,显著高于胰蛋白酶和胃蛋白酶酶解制备得到的肠粘膜蛋白粉可溶性蛋白含量,最佳酶解工艺条件为:水解时间6.5 h,酶添加量5400 U/g蛋白,液固比4 mL/g,在此条件下酶解产物中可溶性蛋白含量为15.81%±0.04%,这表明酶法制备肠粘膜蛋白粉工艺合理可行,为动物副产物的开发利用提供参考依据。 相似文献
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研究逆流超声预处理大米蛋白对其碱性蛋白酶酶解制备血管紧张素转换酶(Angiotensin-I Converting Enzyme,ACE)抑制肽的影响。首先从米渣中提取大米蛋白,以ACE抑制率为主要指标,水解度为辅助指标,运用单因素逐级优化法对酶解反应的底物浓度、时间、温度、加酶量和pH进行参数优化,在此基础上筛选逆流超声模式的最佳超声参数。结果表明最佳酶解参数为底物浓度30 g/L、加酶量(E/S)7.5%、温度50 ℃、pH8.5和酶解时间60 min,此时酶解产物ACE抑制率为45.59%,水解度为21.49%。最佳超声参数为超声频率20 kHz、功率密度170 W/L、时间12.5 min。此时酶解液ACE抑制率达72.24%,水解度为21.64%,相较于未超声组ACE抑制率提高了57.42%,相较于传统超声组,ACE抑制率提高了11.36%。结果表明逆流超声波辅助酶解法能有效提高酶解效率、减少能耗、促进ACE抑制肽制备。 相似文献
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本实验以广东大宗低值沙丁鱼为原料,采用不同蛋白酶降解沙丁鱼以筛选合适的酶组合,然后对原料的酶解制备血管紧张素转化酶(ACE)抑制肽的工艺进行研究。结果表明,制备沙丁鱼ACE抑制肽的酶组合为:木瓜蛋白酶与碱性蛋白酶;酶解的最佳工艺参数为:第一步采用木瓜蛋白酶进行酶解,酶解温度70℃、p H7.5、反应时间2.25 h、酶添加量4000 U/g、料液比30%(w/v);采用碱性蛋白酶进行第二步酶解,酶解温度70℃、p H10.0、反应时间2.0 h、酶添加量5000 U/g。通过工艺优化,沙丁鱼蛋白质的水解度提高到28.44%,并且最终水解蛋白肽的ACE抑制率为73.44%。 相似文献
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通过碱性蛋白酶进行第一步酶解,胰蛋白酶、风味蛋白酶、木瓜蛋白酶和胃蛋白酶分别进行第二步酶解制备鱼鳞明胶抗氧化肽。结果表明,二步酶解法能有效提高酶解物的水解度,降低水解物的分子量,碱性蛋白酶—胰蛋白酶水解物具有显著的自由基清除能力和Fe~(2+)螯合能力。通过响应面优化的胰蛋白酶最佳二步酶解工艺为:底物浓度100 mg/mL、pH 7.8、温度53℃、时间50min,该条件下制备的水解物的Fe~(2+)螯合率为65.72%,清除DPPH·、·OH和O_2~-·的IC_(50)值分别是7.39,0.68,1.84mg/mL。 相似文献