小麦种子过氧化物酶WP1的研究及其对面团流变学特性的影响
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摘要
面粉是众多食品加工的主要原料,如何改善面粉的加工性能是当前小麦育种和食品加工领域的研究热点。育种研究者希望通过改变面粉中各种组分的含量改变面粉的加工性能,而食品加工研究者则希望通过在面粉中添加外源添加剂改变面粉的性质。小麦过氧化物酶1(Wheat Peroxidase 1, WP1)属于含血红素的III型植物过氧化物酶,是小麦种子中主要的过氧化物酶,催化以H202为电子受体的氧化过程；根据其催化性质小麦内源酶WP1可能具有改善面粉加工品质的潜能；然而关于该酶的分离鉴定、体外表达、在种子成熟过程中的生物学功能及其对面粉加工性能影响的研究尚未见报道。
本研究利用柱层析技术从小麦种子中(全麦粉)分离纯化获得WP1,对其酶学性质进行系统分析,并通过掺粉实验研究了其对面粉加工性能的影响；克隆了WP1对应基因,并对其在种子发育过程中的表达谱及组织定位进行了细致研究；而通过原核和酵母表达系统获得具有活性的重组蛋白。具体研究及其结果如下：
1.经水抽提、硫酸铵分级沉淀、阳离子交换层析及凝胶过滤层析从小麦面粉中纯化到一种主要的阳离子过氧化物酶WP1,最终的纯化倍数为154倍,回收率为8.7%；SDS-PAGE显示获得的目的蛋白相对分子量为36 kDa,以ABTS为底物该纯酶的比活力是2174 U·mg-1蛋白。小麦种子过氧化物酶WP1对ABTS、阿魏酸和N-乙酰酪氨酸三种底物有催化作用,最适pH值分别为4.15、5.45和6.30；其中对ABTS和阿魏酸催化效率比N-乙酰酪氨酸高；具有较好的热稳定性；催化活力受钙离子激活和EDTA抑制。
2.通过添加DMSO和甜菜碱,利用RT-PCR的方法克隆到小麦种子特异表达过氧化物酶wpl基因的cDNA。wp1基因cDNA编码一种包含358个氨基酸残基的前体蛋白,其序列与大麦BP1相似性高达92%。空间结构预测结果表明,小麦WP1属于III型过氧化物酶,具有该家族成员典型的血红素和钙离子结合位点。
3.通过向基础面粉中添加WP1、H2O2、Ca2+及EDTA四种物质的七种组合添加物,进行粉质特性测试。结果发现与对照相比,添加H2O2后面团的形成时间、稳定时间和粉质质量指数显著提高,而H2O2对面团特性的改善作用受Ca2+的促进和EDTA的抑制；与单加H202相比,同时添加WP1和H2O2后面团的形成时间、稳定时间和粉质质量指数的提高更加显著,同样这种对面团特性的改善作用受Ca2+的促进和EDTA的抑制。该结果表明WP1可以改善面团的加工性能,但这种改善作用依赖于电子受体H202的存在。
4.利用原核表达系统实现了WP1融合蛋白的高效表达。本研究构建了MBP和His-Tag融合的两种表达载体,诱导表达获得MBP融合的WP1主要以可溶形式存在,表达量达到总蛋白的34.6%；通过直链淀粉亲和层析获得的MBP-WPl融合蛋白,以ABTS底物可检测到过氧化物酶活性。诱导表达获得His-Tag融合的WP1主要以包涵体形式存在,利用Ni-NTA亲和层析柱在变性条件下进行纯化,获得的His-Tag融合WP1经尿素梯度透析复性溶解后免疫新西兰大白兔,最终获得WP1多克隆抗体。ELISA分析结果显示制备的WP1兔抗血清的效价大于1：625000；Western blotting实验结果证明制备的多克隆抗体对WP1具有很好的专一性。
5.通过实时定量PCR和Western blotting的方法,从转录水平和翻译水平研究WPl在种子发育过程中的表达模式。在小麦种子发育初期Wp1表达量相对较低,随着时间延长,wp1基因的表达量持续快速增加,至第13天达到最大值,随后维持一个较高水平；Western blotting结果显示在小麦种子成熟过程中WP1连续累积。应用免疫荧光技术分析了WP1的组织定位,发现WP1主要分布在胚乳细胞和糊粉层细胞的细胞壁中。
6.通过构建乳酸克鲁维酵母和毕赤酵母表达载体pPKLAC-WP1和pPIC9k-WP1,经高效转化、筛选鉴定、诱导表达,获得了含有多拷贝wp1的乳酸克鲁维酵母菌株GG799/pKLAC1-WP1,其分泌蛋白中包含活性的WP1,在含半乳糖的培养基中分泌的WP1是葡萄糖培养基的2倍左右,每升菌液总过氧化物酶活力最大为1050 U；同时获得了含有重组wp1基因的毕赤酵母菌株GS115/pPIC9k-WP1,通过对诱导表达条件的优化,重组菌株在起始菌液浓度为1.5OD,1%甲醇诱导96小时后WP1的表达量为26 mg/L,利用Ni-NTA亲和层析纯化获得His-tag融合的WP1。
本论文从蛋白纯化、基因克隆、原核表达纯化、抗体制备、酵母表达纯化、表达谱分析、免疫荧光组织定位和掺粉测定粉质参数等方面,对小麦种子过氧化物酶WP1进行了系统研究。首次证明内源过氧化物酶WP1可改善小麦面团流变学特性,并阐明了WP1影响面粉加工性能的模式。实现了WP1在两种酵母中的表达,为该酶的生产及应用奠定了基础,也为通过将该基因导入面包酵母改善面包品质设想的实现铺平了道路。
Wheat flour is the ideal raw material for many food products. Recent years, how to improve its dough and breadmaking quality has become a research hotspot in the field of wheat breeding and food industry. The breeders attempt to improve flour processing quality by changing the components of wheat grain and their quantity; and the researchers of food industry attempt to incorporating exogenous components which alter the functionality of dough. Wheat peroxidase 1 is a major peroxidase of wheat grain, which is present in all wheat varieties. WP1 is a typical class III peroxidase which can catalyze the conversion of a large number of phenolic compounds. But, the exact enzymatic property, biological function of WP1 is still unknown. The question we try to give an answer in this thesis is that how WP1 effect on seed developing and dough properties.
In this study, WP1 was purified to homogeneity by chromatography, its catalytic properties was analyzed completely, and its effects on flour processing was analyzed by farinograph tests. The cDNA of wheat peroxidase 1(wp1) was cloned and its expression pattern and tissue location during seed developing was analyzed carefully. The gene of WP1 was expressed in E. coli, P. pastoris and K. lactis system, and the functional recombinant enzyme was obtained by affinity purification. The results were listed as below:
1、The wheat grain major peroxidase WP1 was step wise purified from flour by water extraction, AMS fractional precipitation, SP HP ion-exchange column chromatography and gel filtration chromatography. The purification resulted in a final enrichment of WP1 by 154-fold, with an activity yield of 8.7%. The final specific activity of WP1 for the H2O2-dependent oxidation of ABTS was 2174 U·mg-1. SDS-PAGE result shows that the molecular weight of WP1 is about 36 kDa. WP1 can catalyze the oxidation of ABTS, Ferulic acid and N-acetyl tyrosine, and the optimal pH for them is 4.15,5.45 and 6.30, respectively. WP1 is thermostability and its peroxidase activity can be promoted by Ca2+.
2、The cDNA of wheat peroxidase 1(wp1) was amplified from immature seeds by RT-PCR. The cDNA of Mp1 codes a protein of 358 amino acids, which has a high sequence similarity(92%) with barley peroxidase 1 (BP1). Predicted structure indicates that WP1 belonged to classⅢperoxidase and it has their typical heme binding site and two Ca2+ binding sites.
3、Farinograph tests were conducted with the base flour and the base flour with addition of seven combinations of WP1、H2O2、Ca2+ and EDTA. We found the combination of H2O2 showed higher values than the control for development time, dough stability and farinograph quality number. This improving effect can be promote by Ca2+ and inhibit by EDTA; the combination of WP1/H2O2 showed remarkable higher values than the combination of H2O2 for development time, dough stability and farinograph quality number. This improving effect can be promote by Ca2+ and inhibit by EDTA too. This indicates WP1 improve the processing properties of flour, and this effect depends on H2O2 as electron acceptor.
4、We obtain the recombination WP1 by expression it in prokaryotic system. In this study we construct His-tag and MBP fusion expression vectors. MBP-WP1 is soluble, and its percentage is up to 34.6%. MBP-WP1 was purified by mylase affinity chromatography and it can catalyze the oxidation of ABTS. His-tagged WP1 existed as inclusion body, and its percentage is up to 18.2%. The target protein was purified by Ni-NTA resin affinity chromatography under denatured condition. Pure WP1 was refolded by gradient urea dialysis, then was mixed with equal volume of adjuvant and used as antigen to immune rabbit to prepare polyclonal antibody. The result of ELISA shows that the titer of rabbit anti-WP1 antiserum is higher than 1:625 000. The result of western blotting demonstrated that the prepared WP1 polyclonal antibody can be used to detect WP1 with high specificity.
5、The expression pattern of WP1 during seed developing was analyzed by real-time quantitative PCR and western blotting. Within the first few days after pollination the expression level of wp1 is relative lower. Soon after, the expression of wpl increased rapidly, and it reach the top at 13th day. Before seeds mature, its expression level keep in higher. Using immunohistochemical localization assay we found that WP1 mainly distributed in the extracellular part of endosperm and aleurone layer cell.
6、The recombinant K. lactis strain with multi-copy of wp1 was obtained. High activity recombinant WP1 was secreted into fermentation liquor (1050 U/L). The specific activity of recombinant protein in culture medium with lactose is two fold of that with glucose. The recombinant P. pastoris strain of wpl was obtained too. Optimized initial concentration of the recombinant strain is 1.5OD, and the optimized concentration of methanol is 1%, the yield of enzyme reach to top 96 h after inducing (8700U/L). His-tag fusion WP1 was purified by Ni-NTA affinity chromatography.
From protein purification to gene cloning, prokaryotic expression, antibody preparation, yeast expression, expression profile analysis, immunohisto-localization assay and farinograph tests, wheat grain peroxidase WP1 was studied widely. We first prove that endogenetic peroxidase WP1 can improve flour processing properties, and give an explanation how WP1 does effect on dough and breadmaking quality. At the same, we first functional expression wp1 in two type of yeast, which indicate we can introduce wp1 into baker's yeast to improve the quality of breadmaking.
本研究利用柱层析技术从小麦种子中(全麦粉)分离纯化获得WP1,对其酶学性质进行系统分析,并通过掺粉实验研究了其对面粉加工性能的影响；克隆了WP1对应基因,并对其在种子发育过程中的表达谱及组织定位进行了细致研究；而通过原核和酵母表达系统获得具有活性的重组蛋白。具体研究及其结果如下：
1.经水抽提、硫酸铵分级沉淀、阳离子交换层析及凝胶过滤层析从小麦面粉中纯化到一种主要的阳离子过氧化物酶WP1,最终的纯化倍数为154倍,回收率为8.7%；SDS-PAGE显示获得的目的蛋白相对分子量为36 kDa,以ABTS为底物该纯酶的比活力是2174 U·mg-1蛋白。小麦种子过氧化物酶WP1对ABTS、阿魏酸和N-乙酰酪氨酸三种底物有催化作用,最适pH值分别为4.15、5.45和6.30；其中对ABTS和阿魏酸催化效率比N-乙酰酪氨酸高；具有较好的热稳定性；催化活力受钙离子激活和EDTA抑制。
2.通过添加DMSO和甜菜碱,利用RT-PCR的方法克隆到小麦种子特异表达过氧化物酶wpl基因的cDNA。wp1基因cDNA编码一种包含358个氨基酸残基的前体蛋白,其序列与大麦BP1相似性高达92%。空间结构预测结果表明,小麦WP1属于III型过氧化物酶,具有该家族成员典型的血红素和钙离子结合位点。
3.通过向基础面粉中添加WP1、H2O2、Ca2+及EDTA四种物质的七种组合添加物,进行粉质特性测试。结果发现与对照相比,添加H2O2后面团的形成时间、稳定时间和粉质质量指数显著提高,而H2O2对面团特性的改善作用受Ca2+的促进和EDTA的抑制；与单加H202相比,同时添加WP1和H2O2后面团的形成时间、稳定时间和粉质质量指数的提高更加显著,同样这种对面团特性的改善作用受Ca2+的促进和EDTA的抑制。该结果表明WP1可以改善面团的加工性能,但这种改善作用依赖于电子受体H202的存在。
4.利用原核表达系统实现了WP1融合蛋白的高效表达。本研究构建了MBP和His-Tag融合的两种表达载体,诱导表达获得MBP融合的WP1主要以可溶形式存在,表达量达到总蛋白的34.6%；通过直链淀粉亲和层析获得的MBP-WPl融合蛋白,以ABTS底物可检测到过氧化物酶活性。诱导表达获得His-Tag融合的WP1主要以包涵体形式存在,利用Ni-NTA亲和层析柱在变性条件下进行纯化,获得的His-Tag融合WP1经尿素梯度透析复性溶解后免疫新西兰大白兔,最终获得WP1多克隆抗体。ELISA分析结果显示制备的WP1兔抗血清的效价大于1：625000；Western blotting实验结果证明制备的多克隆抗体对WP1具有很好的专一性。
5.通过实时定量PCR和Western blotting的方法,从转录水平和翻译水平研究WPl在种子发育过程中的表达模式。在小麦种子发育初期Wp1表达量相对较低,随着时间延长,wp1基因的表达量持续快速增加,至第13天达到最大值,随后维持一个较高水平；Western blotting结果显示在小麦种子成熟过程中WP1连续累积。应用免疫荧光技术分析了WP1的组织定位,发现WP1主要分布在胚乳细胞和糊粉层细胞的细胞壁中。
6.通过构建乳酸克鲁维酵母和毕赤酵母表达载体pPKLAC-WP1和pPIC9k-WP1,经高效转化、筛选鉴定、诱导表达,获得了含有多拷贝wp1的乳酸克鲁维酵母菌株GG799/pKLAC1-WP1,其分泌蛋白中包含活性的WP1,在含半乳糖的培养基中分泌的WP1是葡萄糖培养基的2倍左右,每升菌液总过氧化物酶活力最大为1050 U；同时获得了含有重组wp1基因的毕赤酵母菌株GS115/pPIC9k-WP1,通过对诱导表达条件的优化,重组菌株在起始菌液浓度为1.5OD,1%甲醇诱导96小时后WP1的表达量为26 mg/L,利用Ni-NTA亲和层析纯化获得His-tag融合的WP1。
本论文从蛋白纯化、基因克隆、原核表达纯化、抗体制备、酵母表达纯化、表达谱分析、免疫荧光组织定位和掺粉测定粉质参数等方面,对小麦种子过氧化物酶WP1进行了系统研究。首次证明内源过氧化物酶WP1可改善小麦面团流变学特性,并阐明了WP1影响面粉加工性能的模式。实现了WP1在两种酵母中的表达,为该酶的生产及应用奠定了基础,也为通过将该基因导入面包酵母改善面包品质设想的实现铺平了道路。
Wheat flour is the ideal raw material for many food products. Recent years, how to improve its dough and breadmaking quality has become a research hotspot in the field of wheat breeding and food industry. The breeders attempt to improve flour processing quality by changing the components of wheat grain and their quantity; and the researchers of food industry attempt to incorporating exogenous components which alter the functionality of dough. Wheat peroxidase 1 is a major peroxidase of wheat grain, which is present in all wheat varieties. WP1 is a typical class III peroxidase which can catalyze the conversion of a large number of phenolic compounds. But, the exact enzymatic property, biological function of WP1 is still unknown. The question we try to give an answer in this thesis is that how WP1 effect on seed developing and dough properties.
In this study, WP1 was purified to homogeneity by chromatography, its catalytic properties was analyzed completely, and its effects on flour processing was analyzed by farinograph tests. The cDNA of wheat peroxidase 1(wp1) was cloned and its expression pattern and tissue location during seed developing was analyzed carefully. The gene of WP1 was expressed in E. coli, P. pastoris and K. lactis system, and the functional recombinant enzyme was obtained by affinity purification. The results were listed as below:
1、The wheat grain major peroxidase WP1 was step wise purified from flour by water extraction, AMS fractional precipitation, SP HP ion-exchange column chromatography and gel filtration chromatography. The purification resulted in a final enrichment of WP1 by 154-fold, with an activity yield of 8.7%. The final specific activity of WP1 for the H2O2-dependent oxidation of ABTS was 2174 U·mg-1. SDS-PAGE result shows that the molecular weight of WP1 is about 36 kDa. WP1 can catalyze the oxidation of ABTS, Ferulic acid and N-acetyl tyrosine, and the optimal pH for them is 4.15,5.45 and 6.30, respectively. WP1 is thermostability and its peroxidase activity can be promoted by Ca2+.
2、The cDNA of wheat peroxidase 1(wp1) was amplified from immature seeds by RT-PCR. The cDNA of Mp1 codes a protein of 358 amino acids, which has a high sequence similarity(92%) with barley peroxidase 1 (BP1). Predicted structure indicates that WP1 belonged to classⅢperoxidase and it has their typical heme binding site and two Ca2+ binding sites.
3、Farinograph tests were conducted with the base flour and the base flour with addition of seven combinations of WP1、H2O2、Ca2+ and EDTA. We found the combination of H2O2 showed higher values than the control for development time, dough stability and farinograph quality number. This improving effect can be promote by Ca2+ and inhibit by EDTA; the combination of WP1/H2O2 showed remarkable higher values than the combination of H2O2 for development time, dough stability and farinograph quality number. This improving effect can be promote by Ca2+ and inhibit by EDTA too. This indicates WP1 improve the processing properties of flour, and this effect depends on H2O2 as electron acceptor.
4、We obtain the recombination WP1 by expression it in prokaryotic system. In this study we construct His-tag and MBP fusion expression vectors. MBP-WP1 is soluble, and its percentage is up to 34.6%. MBP-WP1 was purified by mylase affinity chromatography and it can catalyze the oxidation of ABTS. His-tagged WP1 existed as inclusion body, and its percentage is up to 18.2%. The target protein was purified by Ni-NTA resin affinity chromatography under denatured condition. Pure WP1 was refolded by gradient urea dialysis, then was mixed with equal volume of adjuvant and used as antigen to immune rabbit to prepare polyclonal antibody. The result of ELISA shows that the titer of rabbit anti-WP1 antiserum is higher than 1:625 000. The result of western blotting demonstrated that the prepared WP1 polyclonal antibody can be used to detect WP1 with high specificity.
5、The expression pattern of WP1 during seed developing was analyzed by real-time quantitative PCR and western blotting. Within the first few days after pollination the expression level of wp1 is relative lower. Soon after, the expression of wpl increased rapidly, and it reach the top at 13th day. Before seeds mature, its expression level keep in higher. Using immunohistochemical localization assay we found that WP1 mainly distributed in the extracellular part of endosperm and aleurone layer cell.
6、The recombinant K. lactis strain with multi-copy of wp1 was obtained. High activity recombinant WP1 was secreted into fermentation liquor (1050 U/L). The specific activity of recombinant protein in culture medium with lactose is two fold of that with glucose. The recombinant P. pastoris strain of wpl was obtained too. Optimized initial concentration of the recombinant strain is 1.5OD, and the optimized concentration of methanol is 1%, the yield of enzyme reach to top 96 h after inducing (8700U/L). His-tag fusion WP1 was purified by Ni-NTA affinity chromatography.
From protein purification to gene cloning, prokaryotic expression, antibody preparation, yeast expression, expression profile analysis, immunohisto-localization assay and farinograph tests, wheat grain peroxidase WP1 was studied widely. We first prove that endogenetic peroxidase WP1 can improve flour processing properties, and give an explanation how WP1 does effect on dough and breadmaking quality. At the same, we first functional expression wp1 in two type of yeast, which indicate we can introduce wp1 into baker's yeast to improve the quality of breadmaking.
引文
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