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Position: Home > Articles > Fermentation Kinetics,Structure and Characteristics of Angiotensin Converting Enzyme Inhibitory Peptides Derived from Bovine Bone FOOD SCIENCE 2017,38 (2) 52-58

牛骨血管紧张素转化酶抑制肽发酵动力学及结构与特性分析

作  者:
刘丽莉;李丹;尹光俊;梁严予;康怀彬
单  位:
河南科技大学食品与生物工程学院
关键词:
蜡样芽孢杆菌;牛骨血管紧张素转化酶抑制肽;发酵动力学;结构表征;特性
摘  要:
前期筛选蜡样芽孢杆菌(Bacillus cereus MBL13-U),结合嗜热链球菌(Streptococcus thermophilus,St)、植物乳杆菌(Lactobacillus plantarum,Lp)混合发酵牛骨粉制备血管紧张素转化酶(angiotensin converting enzyme,ACE)抑制肽,对其发酵动力学进行研究,采用Logistic和Luedeking-Piret等方程对发酵过程进行非线性拟合,建立发酵过程中菌体生长、产物生成、基质消耗动力学模型,拟合度均高于0.97。通过扫描电镜、紫外扫描、差示扫描量热仪对ACE抑制肽进行结构表征。结果表明,由于牛骨ACE抑制肽具有良好的吸湿性,其在扫描电镜下表面出现明显的沟壑痕迹;在222 nm波长处出现强吸收峰,符合胶原多肽的特征吸收;与牛骨胶原蛋白相比,其热变性温度升高,热稳定性较强。同时对其特性分析表明,牛骨ACE抑制肽具有较好的溶解性、较强的耐酸碱性,在0.9 mol/L以内的NaCl浓度条件下耐盐性较强,胃肠道酶对牛骨ACE抑制肽的影响较小。
译  名:
Fermentation Kinetics,Structure and Characteristics of Angiotensin Converting Enzyme Inhibitory Peptides Derived from Bovine Bone
作  者:
LIU Lili;LI Dan;YIN Guangjun;LIANG Yanyu;KANG Huaibin;College of Food and Bioengineering,Henan University of Science and Technology;
关键词:
Bacillus cereus MBL13-U;;angiotensin converting enzyme(ACE) inhibitory peptides;;fermentation kinetic models;;structure characterization;;characteristics
摘  要:
In this work, we conducted a kinetic study on the mixed culture fermentation of bovine bone meal with Bacillus cereus MBL13-U, which was isolated in our previous study, Streptococcus thermophilus and Lactobacillus plantarumfor preparing angiotensin converting enzyme(ACE) inhibitory peptides. Kinetic models with a determination coefficient greater than 0.97 for cell growth, product formation and substrate consumption were developed through nonlinear fitting using Logistic equation and Luecleking-Piret equation. The model predictions were in good agreement with the measured values. The structural properties of the ACE inhibitory peptides were characterized by scanning electron microscopy(SEM), ultraviolet(UV) spectroscopy and differential scanning calorimetry(DSC). The results showed that gully marks appeared on the surface of bovine bone-derived ACE inhibitory peptides, because they had a strong moisture absorption capacity with the maximum absorption at 222 nm as collagen-derived peptides do. Besides, the ACE inhibitory peptides had an increased thermal denaturation temperature and a better thermal stability than bovine bone collagen, apart from good solubility, acid and alkali resistance, and their salt tolerance was strong when the NaCl concentration was below 0.9 mol/L. Pepsin and trypsin had slight effects on bovine bone ACE inhibitory peptides.

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