动态高压微射流技术对酶的活性与构象变化的影响
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摘要
动态高压微射流(DHPM)是一种新兴的非热技术,集高速撞击、高频振荡、瞬时压降、高速剪切和气穴作用于一体,压力可高达200MPa,这种新技术不仅基于高压能力,并且基于不同几何学设计的反应腔(chamber)而获得10—15倍传统阀式均质机,连续操作费时短也不同于静高压。本课题旨在研究DHPM对多酚氧化酶、胰蛋白酶和木瓜蛋白酶的活性与构象变化的影响,尤其关注的是在去折叠态下酶学性质、动力学、稳定性和构象变化的分子机理。
本文研究了中国早酥梨多酚氧化酶的酶学性质和动力学,以邻苯二酚为底物,测得其V_(max)为289.2units/min和K_m为3.8mmol/L,表明早酥梨多酚氧化酶对邻苯二酚具有较高的亲和性;催化反应速率与其浓度成正比;最适pH和温度分别为4.5和45℃。研究了DHPM对早酥梨多酚氧化酶活性影响,表明随着处理压力增加,相对活性从未处理的100%升高至180MPa的182.5%;同等压力下,相对活性随着处理次数的增加而增加;酶液温度(25、35和45℃)在120和140MPa处理条件下影响较大。
DHPM对香菇多酚氧化酶处理也是活性升高。处理压力和次数对香菇多酚氧化酶有显著影响,在110MPa处理一次,其相对活性最高达110.7%;在150MPa处理1-3次,其相对活性分别增加10.4%、10.9%和11.57%,处理3次后相对活性为111.5%。研究了香茹多酚氧化酶的活性与分子构象的机理,圆二色谱显示其二级结构如α-helix遭到破坏,揭示相对活性的提高与其α-helix含量下降有关,荧光光谱显示香茹多酚氧化酶的Trp和Tyr残基或多或少暴露于溶剂中,这一结果与紫外光谱分析相符,巯基测定表明香菇多酚氧化酶表面的巯基基团含量增加。我们发现经DHPM处理后,香茹多酚氧化酶二级结构发生改变,分子构象处于去折叠态。
DHPM对胰蛋白酶的活性没有显著影响,80、100、120和160MPa处理后,胰蛋白酶相对活性分别保留98.5%、98.3%、97.8%和97%。但DHPM处理显著提高了胰蛋白酶的热稳定性和pH稳定性,表现在:45℃保温100min后,未经处理的胰蛋白酶残留活性为86%,而经DHPM 80MPa处理的胰蛋白酶残留活性为96%;DHPM对胰蛋白酶最适pH值没影响,而经DHPM 80、100和120MPa处理后,胰蛋白酶在最适pH(pH=7.6)的活性有所提高,相对活性分别为97%,102%及103%。对胰蛋白酶构象变化分析表明,动态高压微射流处理后胰蛋白酶荧光强度增强、游离巯基含量增加,总巯基含量减少、紫外吸收强度减弱、α-helix强度减弱。这说明DHPM处理导致胰蛋白酶的分子构象部分去折叠态。这一成果进一步印证我们关于天然热力学最稳态不一定是其活性最高态的理论假设。
胰蛋白酶经DHPM处理后构象部分去折叠态导致其反应稳定性增强。根据热动力学假设,去折叠态的胰蛋白酶并不是处在能量最低状态,而是处于一种热力学不稳定的过渡态,随时可能进行refolding或聚集而丧失其反应稳定性。我们提出新的设想:在酶(或蛋白质)的过渡性构象中,通过Patchthe surface(补丁法)、Dowel the exposed amino acid(桩法)、Wedge in gapbetween amino acids(楔法)三种方式来固定其不稳态的去折叠态构象从而维持其更高活性的策略和理论设想。本实验采用mPEG-SC修饰即补丁法策略,结果表明:与天然胰蛋白酶(NT)相比,经DHPM处理后unfolding胰蛋白酶(DT)经mPEG-SC修饰后(NT_P、DT_p),其储存稳定性和热稳定性显著增强。在4℃贮存8后,NT和NT_p变化不大,分别保持61%和59.9%;80和100MPa不同压力处理下经mPEG-SC修饰的D_(80)T_P和D_(100)T_P相对活性分别保持在78%和74%,而未修饰的D_(80)T和D_(100)T相对活性分别陡降到56.5%和50%;热稳定性方面,55℃处理10min后,D_(80)T_P和D_(100)T_P相对活性均保持在87%左右,而D_(80)T和D_(100)T仅存70%的相对活性。目前学术界对热稳定性机理没有统一的解释,认为导致酶或蛋白质热稳定性的原因主要有以下几个方面:表面疏水性/亲水性的变化、表面电荷分布的变化、热变性速率和自水解速率的降低、氢键的形成及解链温度的降低。本实验表明mPEG-SC修饰后,去折叠的胰蛋白酶分子内残基之间的相互作用以及残基和介质之间的相互作用发生了变化,导致去折叠胰蛋白酶的分子构象发生变化,可能是其热稳定性增强的原因。
比较分析DHPM不同chamber(美国Microfluidics公司M-chamber和中国廊坊通用机械公司的反应腔L-chamber)对木瓜蛋白酶性质和构象变化影响的结果表明,两种chamber都导致木瓜蛋白酶活性降低,巯基含量升高。160MPa下处理三次后,M-chamber处理的木瓜蛋白酶(MP)相对活性降低至76.02%,巯基含量增加至110.89%,而L-chamber处理的木瓜蛋白酶(LP)相对活性保留在86.28%,巯基含量为105.36%;MP紫外吸收峰发生蓝移,酪氨酸和色氨酸的荧光最大发射峰红移而LP紫外吸收和荧光光谱几乎没有变化。实验表明在相同的处理压力和处理条件下,不同的chamber仍会导致木瓜蛋白酶产生不同的性质和构象变化,从而证实了我们所提出的“伪压”现象。
通过PyMOLWin软件构造出天然木瓜蛋白酶三维结构模式。在此基础上并根据实验中测得的去折叠态木瓜蛋白酶的构象变化,预测了M-chambers处理后去折叠态木瓜蛋白酶的三维结构图。与天然木瓜蛋白酶相比,去折叠态木瓜蛋白酶结构更加松散、二硫键断裂、酪氨酸和色氨酸残基暴露、α-helix含量降低。
Dynamic High-pressure microfluidization (DHPM) is an emerging nonthermal technology, which uses the combined forces of high-velocity impact, high-frequency vibration, instantaneous pressure drop, intense shear, cavitation, and ultra-high pressures up to 200 MPa. This new technology is based on a very high pressure capacity as well as on a new different reaction chamber geometry design, which can attain pressures 10-15 times higher than classical valve homogenizers. It operations where high pressures are experienced over very short times are different from static high pressures systems.The objective of this investigation was to determine the effect of DHPM on the activity and conformational changes of enzyme (polyphenoloxidase, trypsin and papain), of specific interest were activity, enzyme kinetics, storage stability and molecular conformation in the unfolding state.
Polyphenoloxidase (PPO) from Chinese pear (Pyrus pyrifolia Nakai) was characterized using catechol as a substrate. PPO had a Vmax of 289.2 units/min and a Km of 3.8 mmol/L, which indicates that P. pyrifolia Nakai PPO has a great affinity for catechol. The catalyzing reaction velocity was proportional to the PPO concentration. The optimum pH and temperature for PPO activity were 4.5 and 45°C, respectively. In addition, an investigation was made on the effect of DHPM of treatment pressure, treatment pass and enzyme solution temperature on P. pyrifolia Nakai PPO. As the treatment pressure increased, the PPO relative activity was elevated from 100% untreated to 182.57% treated at 180 MPa. PPO relative activity was enhanced as the treatment pass increased. PPO solution temperature (25, 35, and 45°C) had a significant effect on PPO relative activity when treated at 120 and 140 MPa.
DHPM could also lead mushroom PPO to activation. Treatment pressures had significant effect on the relative activity of mushroom PPO. The highest relative activity of 110.74% was exhibited after one pass treatment at the pressure of 110 MPa.When the enzyme solution was subjected to the pressure of 150 MPa 1, 2 and 3 passes, mushroom PPO was activated by 10.4%, 10.9% and 11.57%, respectively. The relative activity was 111.57% after treated three passes. The relasionship between activity and conformational change had also been investigated.The circular dichroism (CD) analysis demonstrated that some of secondary structures such asα-helix were destroyed. There were some indices that the increase of relative activity was accompanied by a decrease inα-helix content. The fluorescence emission spectra analysis indicated that Trp and Tyr residues in mushroom PPO were more or less exposed to solvent, and the result was in good agreement with that of UV absorption spectra analysis. The sulphydryl groups detection showed that the sulphydryl groups content on the surface of mushroom PPO was increased. We have found that the secondary conformation of mushroom PPO is changed by DHPM treatment and it is in an unfolding state.
DHPM treatment on the activity of trypsin showed no significance; with the relative activity of 98.5% (80 MPa), 98.3% (100 MPa), 97.8% (120 MPa) and 97% (160MPa). However, DHPM treatment enhanced the pH and thermal stability of trypsin. After 100 min of incubation at 45℃, the residual activity of trypsin treated at 80 MPa was still as high as 96% while the untreated trypsin retained only 86% of its original activity. The optimum pH of trypsin maintained surprising consistency (pH=7.6), nevertheless, its relative activity was about 97%, 102% and 103% at 80, 100 and 120 MPa, respectively. In addition, DHPM-induced conformational changes of trypsin were observed. The unfolding of trypsin induced by DHPM treatment was reflected in the increase in maximum emission fluorescence intensity and exposed SH contents as well as the decrease in total SH contents, UV absorbance andα-helix intensity.
The unfolding trypsin induced by DHPM treatment had enhanced stability. However, according to thermodynamic hypothesis, the unfolding trypsin was in a transitional state and will refold or aggregate to be in the lowest energy state. In our opinion, patching the surface, doweling the exposed amino acid, or wedging in gap between amino acids all can stabilize the unfolding state. In this study, mPEG-SC was chosen to react with unfolding trypsin to patch the exposed surface. The result indicated that mPEG-SC showed significant effect on storage stability and thermal stability of DHPM-induced unfolding trypsin in comparison with that of native trypsin although the activity of both was not notably influenced. After storage at 4℃for 8 days, the activity of NT and NT_P remained 61% and 59.9%, respectively, the activity of D_(80)T_P and D_(100)T_P remained still 78% and 74% while the activity of D_(80)T and D_(100)T decreased sharply to 56.5% and 50%. As to thermal stability, D_(80)T_P and D_(100)T_P both remained still approximately 87% of the original activity at 55℃for 10 min in contrast the activity of D_(80)T and D_(100)T only remained 70%.Different explanations for thermal stability mechanism included change of surface hydrophobic/hydrophilic character and surface electric charge distribution, decrease in thermal denaturation and autolysis rate, formation of hydrogen bond, and lowering of the melting temperature of unfolding. The unfolding trypsin modified by mPEG-SC showed higher thermal stability might be due to the conformational change induced by the change of interactions between residues as well as residues and medium.
Activity and conformational changes of papain treated by DHPM with M-chambers and L-chambers were observed. Both chambers resulted in the decrease in activity and the formation of SH group. Under the same condition of 160 MPa for three passes, the activity and total SH content of papain treated by M-chambers was 76.02% and 110.89%, while that of papain treated by L-chambers was 86.28% and 105.36%, respectively. Meanwhile, a violet-shifting of UV absorption peaks and red shift of maximum emission wavelength of Tyr and Trp residues were observed in papain treated by M-chamber, while the UV absorption and fluorescence spectra of papain treated by L-chambers remained unchanged. The phenomenon indicated that in spite of the same treatment pressures and passes, DHPM with different reaction chamber brought about different effect on the characteristics and conformational change of papain. The result proved what we call pseudo-pressure phenomenon.
The three-dimensional structure of native papain was modeled by software of PyMOLWin based on the computational method of de novo structure prediction, and that of unfolding papain induced by DHPM with M-chambers was also predicted and simulated on the basis of conformational change we observed. Differences focused on more "loose" structure、rupture of S-S bonding、exposure of Tyr and Trp residues, and reduction ofα-helix content.
本文研究了中国早酥梨多酚氧化酶的酶学性质和动力学,以邻苯二酚为底物,测得其V_(max)为289.2units/min和K_m为3.8mmol/L,表明早酥梨多酚氧化酶对邻苯二酚具有较高的亲和性;催化反应速率与其浓度成正比;最适pH和温度分别为4.5和45℃。研究了DHPM对早酥梨多酚氧化酶活性影响,表明随着处理压力增加,相对活性从未处理的100%升高至180MPa的182.5%;同等压力下,相对活性随着处理次数的增加而增加;酶液温度(25、35和45℃)在120和140MPa处理条件下影响较大。
DHPM对香菇多酚氧化酶处理也是活性升高。处理压力和次数对香菇多酚氧化酶有显著影响,在110MPa处理一次,其相对活性最高达110.7%;在150MPa处理1-3次,其相对活性分别增加10.4%、10.9%和11.57%,处理3次后相对活性为111.5%。研究了香茹多酚氧化酶的活性与分子构象的机理,圆二色谱显示其二级结构如α-helix遭到破坏,揭示相对活性的提高与其α-helix含量下降有关,荧光光谱显示香茹多酚氧化酶的Trp和Tyr残基或多或少暴露于溶剂中,这一结果与紫外光谱分析相符,巯基测定表明香菇多酚氧化酶表面的巯基基团含量增加。我们发现经DHPM处理后,香茹多酚氧化酶二级结构发生改变,分子构象处于去折叠态。
DHPM对胰蛋白酶的活性没有显著影响,80、100、120和160MPa处理后,胰蛋白酶相对活性分别保留98.5%、98.3%、97.8%和97%。但DHPM处理显著提高了胰蛋白酶的热稳定性和pH稳定性,表现在:45℃保温100min后,未经处理的胰蛋白酶残留活性为86%,而经DHPM 80MPa处理的胰蛋白酶残留活性为96%;DHPM对胰蛋白酶最适pH值没影响,而经DHPM 80、100和120MPa处理后,胰蛋白酶在最适pH(pH=7.6)的活性有所提高,相对活性分别为97%,102%及103%。对胰蛋白酶构象变化分析表明,动态高压微射流处理后胰蛋白酶荧光强度增强、游离巯基含量增加,总巯基含量减少、紫外吸收强度减弱、α-helix强度减弱。这说明DHPM处理导致胰蛋白酶的分子构象部分去折叠态。这一成果进一步印证我们关于天然热力学最稳态不一定是其活性最高态的理论假设。
胰蛋白酶经DHPM处理后构象部分去折叠态导致其反应稳定性增强。根据热动力学假设,去折叠态的胰蛋白酶并不是处在能量最低状态,而是处于一种热力学不稳定的过渡态,随时可能进行refolding或聚集而丧失其反应稳定性。我们提出新的设想:在酶(或蛋白质)的过渡性构象中,通过Patchthe surface(补丁法)、Dowel the exposed amino acid(桩法)、Wedge in gapbetween amino acids(楔法)三种方式来固定其不稳态的去折叠态构象从而维持其更高活性的策略和理论设想。本实验采用mPEG-SC修饰即补丁法策略,结果表明:与天然胰蛋白酶(NT)相比,经DHPM处理后unfolding胰蛋白酶(DT)经mPEG-SC修饰后(NT_P、DT_p),其储存稳定性和热稳定性显著增强。在4℃贮存8后,NT和NT_p变化不大,分别保持61%和59.9%;80和100MPa不同压力处理下经mPEG-SC修饰的D_(80)T_P和D_(100)T_P相对活性分别保持在78%和74%,而未修饰的D_(80)T和D_(100)T相对活性分别陡降到56.5%和50%;热稳定性方面,55℃处理10min后,D_(80)T_P和D_(100)T_P相对活性均保持在87%左右,而D_(80)T和D_(100)T仅存70%的相对活性。目前学术界对热稳定性机理没有统一的解释,认为导致酶或蛋白质热稳定性的原因主要有以下几个方面:表面疏水性/亲水性的变化、表面电荷分布的变化、热变性速率和自水解速率的降低、氢键的形成及解链温度的降低。本实验表明mPEG-SC修饰后,去折叠的胰蛋白酶分子内残基之间的相互作用以及残基和介质之间的相互作用发生了变化,导致去折叠胰蛋白酶的分子构象发生变化,可能是其热稳定性增强的原因。
比较分析DHPM不同chamber(美国Microfluidics公司M-chamber和中国廊坊通用机械公司的反应腔L-chamber)对木瓜蛋白酶性质和构象变化影响的结果表明,两种chamber都导致木瓜蛋白酶活性降低,巯基含量升高。160MPa下处理三次后,M-chamber处理的木瓜蛋白酶(MP)相对活性降低至76.02%,巯基含量增加至110.89%,而L-chamber处理的木瓜蛋白酶(LP)相对活性保留在86.28%,巯基含量为105.36%;MP紫外吸收峰发生蓝移,酪氨酸和色氨酸的荧光最大发射峰红移而LP紫外吸收和荧光光谱几乎没有变化。实验表明在相同的处理压力和处理条件下,不同的chamber仍会导致木瓜蛋白酶产生不同的性质和构象变化,从而证实了我们所提出的“伪压”现象。
通过PyMOLWin软件构造出天然木瓜蛋白酶三维结构模式。在此基础上并根据实验中测得的去折叠态木瓜蛋白酶的构象变化,预测了M-chambers处理后去折叠态木瓜蛋白酶的三维结构图。与天然木瓜蛋白酶相比,去折叠态木瓜蛋白酶结构更加松散、二硫键断裂、酪氨酸和色氨酸残基暴露、α-helix含量降低。
Dynamic High-pressure microfluidization (DHPM) is an emerging nonthermal technology, which uses the combined forces of high-velocity impact, high-frequency vibration, instantaneous pressure drop, intense shear, cavitation, and ultra-high pressures up to 200 MPa. This new technology is based on a very high pressure capacity as well as on a new different reaction chamber geometry design, which can attain pressures 10-15 times higher than classical valve homogenizers. It operations where high pressures are experienced over very short times are different from static high pressures systems.The objective of this investigation was to determine the effect of DHPM on the activity and conformational changes of enzyme (polyphenoloxidase, trypsin and papain), of specific interest were activity, enzyme kinetics, storage stability and molecular conformation in the unfolding state.
Polyphenoloxidase (PPO) from Chinese pear (Pyrus pyrifolia Nakai) was characterized using catechol as a substrate. PPO had a Vmax of 289.2 units/min and a Km of 3.8 mmol/L, which indicates that P. pyrifolia Nakai PPO has a great affinity for catechol. The catalyzing reaction velocity was proportional to the PPO concentration. The optimum pH and temperature for PPO activity were 4.5 and 45°C, respectively. In addition, an investigation was made on the effect of DHPM of treatment pressure, treatment pass and enzyme solution temperature on P. pyrifolia Nakai PPO. As the treatment pressure increased, the PPO relative activity was elevated from 100% untreated to 182.57% treated at 180 MPa. PPO relative activity was enhanced as the treatment pass increased. PPO solution temperature (25, 35, and 45°C) had a significant effect on PPO relative activity when treated at 120 and 140 MPa.
DHPM could also lead mushroom PPO to activation. Treatment pressures had significant effect on the relative activity of mushroom PPO. The highest relative activity of 110.74% was exhibited after one pass treatment at the pressure of 110 MPa.When the enzyme solution was subjected to the pressure of 150 MPa 1, 2 and 3 passes, mushroom PPO was activated by 10.4%, 10.9% and 11.57%, respectively. The relative activity was 111.57% after treated three passes. The relasionship between activity and conformational change had also been investigated.The circular dichroism (CD) analysis demonstrated that some of secondary structures such asα-helix were destroyed. There were some indices that the increase of relative activity was accompanied by a decrease inα-helix content. The fluorescence emission spectra analysis indicated that Trp and Tyr residues in mushroom PPO were more or less exposed to solvent, and the result was in good agreement with that of UV absorption spectra analysis. The sulphydryl groups detection showed that the sulphydryl groups content on the surface of mushroom PPO was increased. We have found that the secondary conformation of mushroom PPO is changed by DHPM treatment and it is in an unfolding state.
DHPM treatment on the activity of trypsin showed no significance; with the relative activity of 98.5% (80 MPa), 98.3% (100 MPa), 97.8% (120 MPa) and 97% (160MPa). However, DHPM treatment enhanced the pH and thermal stability of trypsin. After 100 min of incubation at 45℃, the residual activity of trypsin treated at 80 MPa was still as high as 96% while the untreated trypsin retained only 86% of its original activity. The optimum pH of trypsin maintained surprising consistency (pH=7.6), nevertheless, its relative activity was about 97%, 102% and 103% at 80, 100 and 120 MPa, respectively. In addition, DHPM-induced conformational changes of trypsin were observed. The unfolding of trypsin induced by DHPM treatment was reflected in the increase in maximum emission fluorescence intensity and exposed SH contents as well as the decrease in total SH contents, UV absorbance andα-helix intensity.
The unfolding trypsin induced by DHPM treatment had enhanced stability. However, according to thermodynamic hypothesis, the unfolding trypsin was in a transitional state and will refold or aggregate to be in the lowest energy state. In our opinion, patching the surface, doweling the exposed amino acid, or wedging in gap between amino acids all can stabilize the unfolding state. In this study, mPEG-SC was chosen to react with unfolding trypsin to patch the exposed surface. The result indicated that mPEG-SC showed significant effect on storage stability and thermal stability of DHPM-induced unfolding trypsin in comparison with that of native trypsin although the activity of both was not notably influenced. After storage at 4℃for 8 days, the activity of NT and NT_P remained 61% and 59.9%, respectively, the activity of D_(80)T_P and D_(100)T_P remained still 78% and 74% while the activity of D_(80)T and D_(100)T decreased sharply to 56.5% and 50%. As to thermal stability, D_(80)T_P and D_(100)T_P both remained still approximately 87% of the original activity at 55℃for 10 min in contrast the activity of D_(80)T and D_(100)T only remained 70%.Different explanations for thermal stability mechanism included change of surface hydrophobic/hydrophilic character and surface electric charge distribution, decrease in thermal denaturation and autolysis rate, formation of hydrogen bond, and lowering of the melting temperature of unfolding. The unfolding trypsin modified by mPEG-SC showed higher thermal stability might be due to the conformational change induced by the change of interactions between residues as well as residues and medium.
Activity and conformational changes of papain treated by DHPM with M-chambers and L-chambers were observed. Both chambers resulted in the decrease in activity and the formation of SH group. Under the same condition of 160 MPa for three passes, the activity and total SH content of papain treated by M-chambers was 76.02% and 110.89%, while that of papain treated by L-chambers was 86.28% and 105.36%, respectively. Meanwhile, a violet-shifting of UV absorption peaks and red shift of maximum emission wavelength of Tyr and Trp residues were observed in papain treated by M-chamber, while the UV absorption and fluorescence spectra of papain treated by L-chambers remained unchanged. The phenomenon indicated that in spite of the same treatment pressures and passes, DHPM with different reaction chamber brought about different effect on the characteristics and conformational change of papain. The result proved what we call pseudo-pressure phenomenon.
The three-dimensional structure of native papain was modeled by software of PyMOLWin based on the computational method of de novo structure prediction, and that of unfolding papain induced by DHPM with M-chambers was also predicted and simulated on the basis of conformational change we observed. Differences focused on more "loose" structure、rupture of S-S bonding、exposure of Tyr and Trp residues, and reduction ofα-helix content.
引文
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