蚕蛹蛋白酶解制备抗氧化和降血压活性产物及其动力学研究
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摘要
蚕蛹作为缫丝企业的主要副产品产量高,由于缺乏深加工技术,大量蚕蛹都作为饲料和肥料使用,资源利用率和附加值低。蚕蛹蛋白质量占干蚕蛹质量的45%-50%,经测定在蚕蛹蛋白中含有18种人体所需的氨基酸,是一种较为理想的优质纯天然全价蛋白质,而蚕蛹蛋白的酶解产物蚕蛹多肽也具有多种功能活性。虽然目前关于蚕蛹蛋白综合利用的研究已有很多,但还存在研究的广度和深度不够的问题,主要体现在蚕蛹蛋白酶解产物功能活性开发和酶解动力学过程研究不够深入等方面。本论文从蚕蛹蛋白的深加工应用研究和蛋白酶解过程基础研究出发,优化蚕蛹蛋白精制工艺,同时优化中性蛋白酶和碱性蛋白酶水解蚕蛹蛋白体系制备具有较高抗氧化和降血压活性酶解产物的工艺,推导两个酶反应体系的宏观动力学方程和集总动力学方程。主要取得以下几方面的研究成果：
对制备得到的蚕蛹蛋白进行氨基酸含量和分子量分布分析,发现蚕蛹蛋白中8种必需氨基酸占总量的48.03%,疏水性氨基酸占总氨基酸含量的46.69%,具有进一步研究其抗氧化和和ACE抑制活性肽的潜力。蚕蛹蛋白水溶液分子量分布结果显示,蚕蛹蛋白中包含有多种蛋白和多肽,分子量范围从90kDa到500Da。
用5种蛋白酶水解蚕蛹蛋白,以O2-·、DPPH-及·OH的抑制率和ACE的抑制率作为抗氧化和降血压活性的测检指标,发现中性蛋白酶和碱性蛋白酶的酶解产物同时具有较强的抗氧化和降血压活性。根据响应面试验设计方法,再以水解度作为响应面指标,得到中性蛋白酶最优条件为反应温度49℃,pH值7.00,加酶量0.70%,反应180min；碱性蛋白酶最优条件为反应温度51℃,pH值9.05,加酶量0.38%,反应180min,并通过实验验证其误差值小于5%,说明采用响应面试验设计方法对蚕蛹蛋白酶解体系进行优化具有较好的可靠性。
结合酶解反应机理推导出中性蛋白酶和碱性蛋白酶水解蚕蛹蛋白体系宏观动力学模型,计算得到两个酶反应体系动力学常数分别为米氏常数4.0g-L-1、产物生成速率常数130.9min-1、底物抑制常数110.4g·L-1、酶失活速率常数24.6min-1(中性蛋白酶)和米氏常数3.5g·L-1、产物生成速率常数251.7min-1、底物抑制常数94.8g·L-1、酶失活速率常数41.4min-1(碱性蛋白酶),证明在两个体系内存在底物抑制现象,其最适底物浓度分别为32.7g·L-1和23.4g·L-1。根据实验验证两个酶反应体系反应模型,平均相对误差分别为3.80%和4.60%。再通过对两个体系不同反应条件下增溶度的分析,建立了增溶度与水解度经验方程。
根据蚕蛹蛋白酶解机理,提出蚕蛹蛋白酶解集总动力学假设,再根据蛋白的溶解性和酶解产物分子量分布情况,建立两个酶反应体系蚕蛹蛋白三集总反应数学模型。测定酶失活速率常数和各集总本征动力学常数后,拟合出集总反应网络动力学参数,建立各动力学常数与开氏温度的关系式,并分析影响速率常数的主要因素,得到相应的反应活化能分别为22.22kJ·mo1-1和9.52kJ·mol-1。为验证模型可靠性,在不同温度下进行实验,结果表明实验值与计算值较为吻合,说明该模型具有较好的推算性。再通过测定不同集总组分的抗氧化和ACE抑制活性发现主要活性都集中在分子量最小组分(集总组分C)中,并通过蚕蛹蛋白宏观动力学模型和集总动力学模型的关联,得到两个酶反应体系水解度、主要集总组分和反应时间关联方程组,为优化生物活性肽的生产工艺提供理论依据。
Silkworm (Bombyx mori) pupae are considered main msilk industry waste. Because of shorting at the technical support, silkworm pupae mostly consumed as animal feed and fertilizer. The protein of silkworm pupae (PSP) alone consists of about40%-60%of the total dry pupae weight, containing18known amino acids and is considered as a good nutritional source of protein. In this thesis, in accordance with the deep processing application and mechanism of protein hydrolysis about PSP, extraction condition was optimized by one-factor for PSP from silkworm pupae. Then the hydrolyzates of PSP catalyzed by neutrase and alacase exerted the higher antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activity. The hydrolyzing conditions were optimized by response surface methodology (RSM). At last, the macro dynamic equation and lumped dynamic equation are deduced about neutrase and alacase reaction system, the main results are as follow.
Amino acid composition and of PSP was analyzed with HPLC. Experiment results show that8essential amino acids (EAA) and hydrophobic amino acid was48.03%and46.69%of total amino, respectively. It is worthwhile to do the further research on antioxidative activity and angiotemin-I-converting enzyme (ACE) inhibitory activity because of its enormous potentials. Molecular weight distribution was obtained by HPSEC. The results indicated that the PSP included a variety of small proteins and peptide with the molecular weight range from500to100000Da.
The hydrolyzates of silkworm pupae protein were catalyzed by neutrase, alcalase, bromelain, trypsin and papain. The ACE inhibitory activity and antioxidative activity were identified by HPLC and spectrophotometry. The hydrolyzates catalyzed by neutrase and alcalase exerted the higher antioxidative activity and inhibitory activity. The hydrolyzing conditions were optimized by one-factor and Box-Behnken design methods, and response surface methodology (RSM). Statistical analyses showed that regression of the second-order model equation is suitable to describe degree of hydrolysis, and the average regressive error was less than5%. The neutrase optimum technology conditions were:hydrolysis temperture at49℃, pH7.00, enzyme concentration0.38%(w/w) and reaction time180min. The alcalase optimum technology conditions were:hydrolysis temperature at51℃, pH9.05, enzyme concentration0.70%(w/w) and reaction time180min. The reliability of the model was verified by RSM, and the average regression error was less than5%.
Taking into account the reaction mechanism, a kinetic model was established to characterize the enzymatic hydrolysis curves about neutrase and alcalase. The reaction constants in neutrase were determined as michaelis constant4.02g·L-1, product formation rate constant130.9min-1, substrate inhibition constant110.4g·L-1and enzyme inactivation rate constant24.6min. The reaction constants in alcalase were determined as michaelis constant3.5g·L-1, product formation rate constant251.7min-1,substrate inhibition constant94.8g·L-1and enzyme inactivation rate constant41.4min-1. It proved that the substrate inhibition existed in neutrase and alcalase system, and its optimum substrate concentration were determined as32.7g·L-1and23.4g·L-1. The experimental data were substituted this kinetic model, the regressive results agree well with the experimental data, i. e. the average relative error was only3.80%and4.60%. The kinetics of hydrolysis and solubilization for all experiments could be represented, and the empirical model was defined and the relationship between hydrolysis and solubilization was power found for all experimental data.
Taking into account the reaction mechanism, this paper applied lumping kinetics to the PSP-neutrase and PSP-alcalase systems. The principle of lumping kinetic was built base on solubility of PSP and molecular weight distribution of hydrolysates. The lumped components of the complex reaction system were defined and a three-lumping reaction network was proposed in two systems. Reaction of the lumps was described with intrinsic kinetic equations, which contained product inhibition; substrate inhibition, enzyme inactivation and the variation of different lumped components in different time, and system of differential equations for this reaction of lumps were established, and its reaction activation energy were determined as22.22kJ-mol-1and9.52kJ-mol-1. The reliability of the model was verified by comparing the computed values with the experimental values, and the kinetic equations could be used to model the hydrolysis process. The functional test of different lumped components showed that it is holds better ACE inhibitory activity and antioxidative activity in lump C. By means of the combination of macro dynamic equation and lumped dynamic equation, system of equations in two systems were deduced about degree of hydrolysis, different lumped components and reaction time. These equations offer the theory support for the technological process of bioactive peptides
对制备得到的蚕蛹蛋白进行氨基酸含量和分子量分布分析,发现蚕蛹蛋白中8种必需氨基酸占总量的48.03%,疏水性氨基酸占总氨基酸含量的46.69%,具有进一步研究其抗氧化和和ACE抑制活性肽的潜力。蚕蛹蛋白水溶液分子量分布结果显示,蚕蛹蛋白中包含有多种蛋白和多肽,分子量范围从90kDa到500Da。
用5种蛋白酶水解蚕蛹蛋白,以O2-·、DPPH-及·OH的抑制率和ACE的抑制率作为抗氧化和降血压活性的测检指标,发现中性蛋白酶和碱性蛋白酶的酶解产物同时具有较强的抗氧化和降血压活性。根据响应面试验设计方法,再以水解度作为响应面指标,得到中性蛋白酶最优条件为反应温度49℃,pH值7.00,加酶量0.70%,反应180min；碱性蛋白酶最优条件为反应温度51℃,pH值9.05,加酶量0.38%,反应180min,并通过实验验证其误差值小于5%,说明采用响应面试验设计方法对蚕蛹蛋白酶解体系进行优化具有较好的可靠性。
结合酶解反应机理推导出中性蛋白酶和碱性蛋白酶水解蚕蛹蛋白体系宏观动力学模型,计算得到两个酶反应体系动力学常数分别为米氏常数4.0g-L-1、产物生成速率常数130.9min-1、底物抑制常数110.4g·L-1、酶失活速率常数24.6min-1(中性蛋白酶)和米氏常数3.5g·L-1、产物生成速率常数251.7min-1、底物抑制常数94.8g·L-1、酶失活速率常数41.4min-1(碱性蛋白酶),证明在两个体系内存在底物抑制现象,其最适底物浓度分别为32.7g·L-1和23.4g·L-1。根据实验验证两个酶反应体系反应模型,平均相对误差分别为3.80%和4.60%。再通过对两个体系不同反应条件下增溶度的分析,建立了增溶度与水解度经验方程。
根据蚕蛹蛋白酶解机理,提出蚕蛹蛋白酶解集总动力学假设,再根据蛋白的溶解性和酶解产物分子量分布情况,建立两个酶反应体系蚕蛹蛋白三集总反应数学模型。测定酶失活速率常数和各集总本征动力学常数后,拟合出集总反应网络动力学参数,建立各动力学常数与开氏温度的关系式,并分析影响速率常数的主要因素,得到相应的反应活化能分别为22.22kJ·mo1-1和9.52kJ·mol-1。为验证模型可靠性,在不同温度下进行实验,结果表明实验值与计算值较为吻合,说明该模型具有较好的推算性。再通过测定不同集总组分的抗氧化和ACE抑制活性发现主要活性都集中在分子量最小组分(集总组分C)中,并通过蚕蛹蛋白宏观动力学模型和集总动力学模型的关联,得到两个酶反应体系水解度、主要集总组分和反应时间关联方程组,为优化生物活性肽的生产工艺提供理论依据。
Silkworm (Bombyx mori) pupae are considered main msilk industry waste. Because of shorting at the technical support, silkworm pupae mostly consumed as animal feed and fertilizer. The protein of silkworm pupae (PSP) alone consists of about40%-60%of the total dry pupae weight, containing18known amino acids and is considered as a good nutritional source of protein. In this thesis, in accordance with the deep processing application and mechanism of protein hydrolysis about PSP, extraction condition was optimized by one-factor for PSP from silkworm pupae. Then the hydrolyzates of PSP catalyzed by neutrase and alacase exerted the higher antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activity. The hydrolyzing conditions were optimized by response surface methodology (RSM). At last, the macro dynamic equation and lumped dynamic equation are deduced about neutrase and alacase reaction system, the main results are as follow.
Amino acid composition and of PSP was analyzed with HPLC. Experiment results show that8essential amino acids (EAA) and hydrophobic amino acid was48.03%and46.69%of total amino, respectively. It is worthwhile to do the further research on antioxidative activity and angiotemin-I-converting enzyme (ACE) inhibitory activity because of its enormous potentials. Molecular weight distribution was obtained by HPSEC. The results indicated that the PSP included a variety of small proteins and peptide with the molecular weight range from500to100000Da.
The hydrolyzates of silkworm pupae protein were catalyzed by neutrase, alcalase, bromelain, trypsin and papain. The ACE inhibitory activity and antioxidative activity were identified by HPLC and spectrophotometry. The hydrolyzates catalyzed by neutrase and alcalase exerted the higher antioxidative activity and inhibitory activity. The hydrolyzing conditions were optimized by one-factor and Box-Behnken design methods, and response surface methodology (RSM). Statistical analyses showed that regression of the second-order model equation is suitable to describe degree of hydrolysis, and the average regressive error was less than5%. The neutrase optimum technology conditions were:hydrolysis temperture at49℃, pH7.00, enzyme concentration0.38%(w/w) and reaction time180min. The alcalase optimum technology conditions were:hydrolysis temperature at51℃, pH9.05, enzyme concentration0.70%(w/w) and reaction time180min. The reliability of the model was verified by RSM, and the average regression error was less than5%.
Taking into account the reaction mechanism, a kinetic model was established to characterize the enzymatic hydrolysis curves about neutrase and alcalase. The reaction constants in neutrase were determined as michaelis constant4.02g·L-1, product formation rate constant130.9min-1, substrate inhibition constant110.4g·L-1and enzyme inactivation rate constant24.6min. The reaction constants in alcalase were determined as michaelis constant3.5g·L-1, product formation rate constant251.7min-1,substrate inhibition constant94.8g·L-1and enzyme inactivation rate constant41.4min-1. It proved that the substrate inhibition existed in neutrase and alcalase system, and its optimum substrate concentration were determined as32.7g·L-1and23.4g·L-1. The experimental data were substituted this kinetic model, the regressive results agree well with the experimental data, i. e. the average relative error was only3.80%and4.60%. The kinetics of hydrolysis and solubilization for all experiments could be represented, and the empirical model was defined and the relationship between hydrolysis and solubilization was power found for all experimental data.
Taking into account the reaction mechanism, this paper applied lumping kinetics to the PSP-neutrase and PSP-alcalase systems. The principle of lumping kinetic was built base on solubility of PSP and molecular weight distribution of hydrolysates. The lumped components of the complex reaction system were defined and a three-lumping reaction network was proposed in two systems. Reaction of the lumps was described with intrinsic kinetic equations, which contained product inhibition; substrate inhibition, enzyme inactivation and the variation of different lumped components in different time, and system of differential equations for this reaction of lumps were established, and its reaction activation energy were determined as22.22kJ-mol-1and9.52kJ-mol-1. The reliability of the model was verified by comparing the computed values with the experimental values, and the kinetic equations could be used to model the hydrolysis process. The functional test of different lumped components showed that it is holds better ACE inhibitory activity and antioxidative activity in lump C. By means of the combination of macro dynamic equation and lumped dynamic equation, system of equations in two systems were deduced about degree of hydrolysis, different lumped components and reaction time. These equations offer the theory support for the technological process of bioactive peptides
引文
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