黄粉虫幼虫蛋白酶解制备降血压肽的研究
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摘要
黄粉虫幼虫体内蛋白、脂肪含量较高，其体内蛋白质含量高达50%（干重）左右，素有“动物蛋白饲料之王”的称誉。由于黄粉虫易于饲养，我国黄粉虫资源非常丰富。长期以来，由于对其缺乏系统研究，开发利用较少，使优质蛋白资源被浪费。目前，利用黄粉虫幼虫体内丰富的蛋白质制备活性肽的研究尚未见报道。本文对脱脂黄粉虫幼虫蛋白Alcalase酶解制备降血压肽进行了系统研究，成功制备出黄粉虫幼虫蛋白降压肽。这一研究为拓宽黄粉虫幼虫的应用范围，开发黄粉虫幼虫蛋白资源开辟了新途径。
采用超临界CO2对黄粉虫幼虫粉进行脱脂，脱脂条件：萃取压力35MPa，萃取温度35℃，萃取时间200min，常压分离。脱脂后总蛋白含量达到60.5%。
脱脂黄粉虫幼虫中清蛋白、球蛋白、醇溶蛋白及谷蛋白含量分别占蛋白总量的9.0%、1.5%、2.3%及23.7%，其中清蛋白及谷蛋白含量较高；另有63.5%的蛋白质残留在残渣中。氨基酸组成分析结果表明，谷蛋白及残渣蛋白中非极性氨基酸和芳香族氨基酸含量较高，这两种蛋白对于黄粉虫幼虫蛋白酶解制备降血压肽贡献较大，为提高蛋白利用率，故在后续试验中直接以脱脂黄粉虫幼虫粉作为酶解原料。
采用蛋白酶对脱脂黄粉虫幼虫蛋白进行水解制备降血压肽。从6种蛋白酶中筛选出Alcalase水解脱脂黄粉虫幼虫蛋白，酶解条件：底物浓度3%，加酶量4000U/g底物，酶解温度50℃，pH8.5，水解度20%时，水解产物对ACE的抑制作用较强，此时酶解液的IC50值为0.39mg/mL。
采用350W/g底物的脉冲超声波对脱脂黄粉虫幼虫蛋白进行预处理，当预处理时间10min时，蛋白酶解至DH20%所用时间缩短20%。通过紫外吸收光谱、荧光发射光谱、蛋白疏水性、游离巯基含量、粒径、圆二色谱及变性聚丙烯酰胺凝胶电泳测定，可知超声波能够引起清蛋白及谷蛋白空间结构改变，但并未改变蛋白质的一级结构。
在脱脂黄粉虫幼虫蛋白水解过程中施加超声波处理（2.5及5min）可以加快水解速率。实验结果表明：短时间超声波处理（5min内）可使Alcalase活性增强，长时间超声波处理会降低其活性；且超声波处理后，Alcalase的紫外吸收光谱及荧光发射光谱发生了改变，说明其结构发生了变化。但超声波处理不能改变水解液（DH8%）的氨基酸组成。
采用活性炭对脱脂黄粉虫幼虫蛋白酶解液进行脱色。脱色后的蛋白酶解液经葡聚糖凝胶G-15分离后得到四个组分（Peak1、Peak2、Peak3及Peak4）。通过对四个组分进行氨基酸组成分析及相对分子质量分布测定，可知Peak2组分更适合用来制备ACE抑制肽。采用高效液相色谱法测定四个组分对ACE的抑制活性，结果表明四个组分的IC50值分别为0.46、0.23、0.83及2.81mg/mL。
采用液相色谱对Peak2进行分离纯化，得到20个组分，其中P2-F6及P2-F9两个组分对ACE的抑制作用较强。对这两个组分进行二次液相色谱分离纯化，采用基质辅助激光解吸电离飞行时间质谱对其中的活性多肽进行结构鉴定。结果表明，从P2-F6中分离得到二肽Ser-Met和三肽Tyr-Ala-Asn，从P2-F9中分离得到二肽Asn-Tyr，其IC50值分别为0.026、0.017及0.011mg/mL，其中Ser-Met和Tyr-Ala-Asn是尚未见报道的降血压肽。
将Peak2组分分别以100、200和400mg/kg体重的剂量对原发性高血压大鼠（SHR）进行一次灌胃，SHR血压下降明显。同时发现脱脂黄粉虫幼虫蛋白酶解物具有一定的抗氧化作用。
Tenebrio molitor (L.) larva is a kind of important and high quality insect resources containing anabundant amount of protein and fat. It has known as “the king of animal protein content” because theprotein content in the body even reached about50%on a dry matter basis. Although the resource ofTenebrio molitor (L.) larva in our country was abundant because of its easily breeding, the lack ofsystematic and reasonable research has limited its utilization. The study of antihypertensive peptides fromTenebrio molitor (L.) larva has not been reported nowadays. Antihypertensive peptides from Tenebriomolitor (L.) larva protein were obtained successfully in the paper. The research can not only broadapplication areas, but also develop new ways for further utilization of Tenebrio molitor (L.) larva protein.
The fat was extracted with supercritical carbon dioxide from Tenebrio molitor (L.) larva. And theextraction conditions were as follows: pressure35MPa, temperature35℃, extracting time200min. Theprotein content then reached60.5%after the fat was removed.
The content of albumin, globulin, alcohol soluble protein and glutenin isolated from defatted Tenebriomolitor (L.) larva was9.0%，1.5%，2.3%and23.7%, respectively. There was still63.5%of proteinremaining in the residue. The amino acids composition of protein fractions indicated that non polar aminoacids and aromatic amino acid was abundant in glutenin and residual protein. In order to improve theutilization efficiency of protein, defatted Tenebrio molitor (L.) larva was used directly as the raw materialsin the experiments.
Alcalase was chosen to prepare antihypertensive peptides from defatted Tenebrio molitor (L.) larvaprotein. The optimum enzymatic conditions were determinated as follows: substrate concentration3%,Alcalase dosage4000U/g substrate, temperature50℃, pH value8.5. The ACE inhibitory activity was thestrongest when hydrolytic degree reached20%. And the IC50value of the hydrolysates was determined at0.39mg/mL.
Ultrasound (350W/g substrate) was used to treat defatted Tenebrio molitor (L.) larva protein beforeenzymatic hydrolysis in the experiment. The hydrolysis time (DH reached20%) was shorted by20%whenpretreated for10min. The effects of ultrasonic treatment on conformation of Tenebrio molitor (L.) larvaprotein were studied by means of ultraviolet absorption spectra, fluorescence emission spectra, surfacehydrophobicity, free sulfhydryl content, particle size distribution, circular dichroism, and sodium dodecylsulphate-polyacrylamide gel electrophoresis. The results indicated that ultrasonic treatment changed theconformation of albumin and glutenin isolated from defatted Tenebrio molitor (L.) larva. But the primarystructure of protein was not affected by ultrasound.
The effects of ultrasound on the enzymatic hydrolysis of defatted Tenebrio molitor (L.) larva proteinwith Alcalase were also investigated. The results indicated that ultrasonic treatment (2.5and5min) canaccelerate the enzymatic hydrolysis procedures of samples. The influence of ultrasound on activity andconformation of Alcalase was also measured. The result revealed enzyme activity was significantlyimproved as being treated for5min, while extensive processing on the contrary decreased the activity ofAlcalase. The results of ultraviolet absorption and fluorescence emission showed that ultrasonic treatmentled to a change on molecular structure of Alcalase. Amino acid composition in hydrolysates (DH8%) ofTenebrio molitor (L.) larva protein was almost the same whether enzymatic hydrolysis was treated withultrasound or not.
Tenebrio molitor (L.) larva protein hydrolysates was fractionated using Sephadex G-15columnchromatography after decolored by activated carbon, four peaks (Peak1，Peak2，Peak3and Peak4) wereobtained. The results of amino acids composition and relative molecular weight distribution indicated that
Peak2was suitable for production of ACE inhibitory peptides. The IC50value of four fractions isolatedusing gel filtration was determined with high performance liquid chromatography. The value was0.46,0.23,0.83and2.81mg/mL, respectively.
The active fractions in Peak2based on the ACE inhibiting activity were isolated and purified byHPLC. P2-F6and P2-F9among20fractions isolated from Peak2were further purified because of theirstrong ACE inhibitory activity. The amino acid sequences of ACE inhibitory peptides were Ser-Met andTyr-Ala-Asn from P2-F6and Asn-Tyr from P2-F9determined by Matrix-Assisted LaserDesorption/Ionization Time of Flight Mass Spectrometry. The IC50value of them was0.026，0.017and0.011mg/mL, respectively. Ser-Met and Tyr-Ala-Asn have not been reported as antihypertensive peptidesyet.
Blood pressure of spontaneously hypertensive rats (SHR) decreased obviously after fed with thefraction of Peak2, in a single oral administration in100,200and400mg/kg.bw dosage respectively. It isalso discovered that defatted Tenebrio molitor (L.) larva protein hydrolysates has some antioxidant effect.
采用超临界CO2对黄粉虫幼虫粉进行脱脂，脱脂条件：萃取压力35MPa，萃取温度35℃，萃取时间200min，常压分离。脱脂后总蛋白含量达到60.5%。
脱脂黄粉虫幼虫中清蛋白、球蛋白、醇溶蛋白及谷蛋白含量分别占蛋白总量的9.0%、1.5%、2.3%及23.7%，其中清蛋白及谷蛋白含量较高；另有63.5%的蛋白质残留在残渣中。氨基酸组成分析结果表明，谷蛋白及残渣蛋白中非极性氨基酸和芳香族氨基酸含量较高，这两种蛋白对于黄粉虫幼虫蛋白酶解制备降血压肽贡献较大，为提高蛋白利用率，故在后续试验中直接以脱脂黄粉虫幼虫粉作为酶解原料。
采用蛋白酶对脱脂黄粉虫幼虫蛋白进行水解制备降血压肽。从6种蛋白酶中筛选出Alcalase水解脱脂黄粉虫幼虫蛋白，酶解条件：底物浓度3%，加酶量4000U/g底物，酶解温度50℃，pH8.5，水解度20%时，水解产物对ACE的抑制作用较强，此时酶解液的IC50值为0.39mg/mL。
采用350W/g底物的脉冲超声波对脱脂黄粉虫幼虫蛋白进行预处理，当预处理时间10min时，蛋白酶解至DH20%所用时间缩短20%。通过紫外吸收光谱、荧光发射光谱、蛋白疏水性、游离巯基含量、粒径、圆二色谱及变性聚丙烯酰胺凝胶电泳测定，可知超声波能够引起清蛋白及谷蛋白空间结构改变，但并未改变蛋白质的一级结构。
在脱脂黄粉虫幼虫蛋白水解过程中施加超声波处理（2.5及5min）可以加快水解速率。实验结果表明：短时间超声波处理（5min内）可使Alcalase活性增强，长时间超声波处理会降低其活性；且超声波处理后，Alcalase的紫外吸收光谱及荧光发射光谱发生了改变，说明其结构发生了变化。但超声波处理不能改变水解液（DH8%）的氨基酸组成。
采用活性炭对脱脂黄粉虫幼虫蛋白酶解液进行脱色。脱色后的蛋白酶解液经葡聚糖凝胶G-15分离后得到四个组分（Peak1、Peak2、Peak3及Peak4）。通过对四个组分进行氨基酸组成分析及相对分子质量分布测定，可知Peak2组分更适合用来制备ACE抑制肽。采用高效液相色谱法测定四个组分对ACE的抑制活性，结果表明四个组分的IC50值分别为0.46、0.23、0.83及2.81mg/mL。
采用液相色谱对Peak2进行分离纯化，得到20个组分，其中P2-F6及P2-F9两个组分对ACE的抑制作用较强。对这两个组分进行二次液相色谱分离纯化，采用基质辅助激光解吸电离飞行时间质谱对其中的活性多肽进行结构鉴定。结果表明，从P2-F6中分离得到二肽Ser-Met和三肽Tyr-Ala-Asn，从P2-F9中分离得到二肽Asn-Tyr，其IC50值分别为0.026、0.017及0.011mg/mL，其中Ser-Met和Tyr-Ala-Asn是尚未见报道的降血压肽。
将Peak2组分分别以100、200和400mg/kg体重的剂量对原发性高血压大鼠（SHR）进行一次灌胃，SHR血压下降明显。同时发现脱脂黄粉虫幼虫蛋白酶解物具有一定的抗氧化作用。
Tenebrio molitor (L.) larva is a kind of important and high quality insect resources containing anabundant amount of protein and fat. It has known as “the king of animal protein content” because theprotein content in the body even reached about50%on a dry matter basis. Although the resource ofTenebrio molitor (L.) larva in our country was abundant because of its easily breeding, the lack ofsystematic and reasonable research has limited its utilization. The study of antihypertensive peptides fromTenebrio molitor (L.) larva has not been reported nowadays. Antihypertensive peptides from Tenebriomolitor (L.) larva protein were obtained successfully in the paper. The research can not only broadapplication areas, but also develop new ways for further utilization of Tenebrio molitor (L.) larva protein.
The fat was extracted with supercritical carbon dioxide from Tenebrio molitor (L.) larva. And theextraction conditions were as follows: pressure35MPa, temperature35℃, extracting time200min. Theprotein content then reached60.5%after the fat was removed.
The content of albumin, globulin, alcohol soluble protein and glutenin isolated from defatted Tenebriomolitor (L.) larva was9.0%，1.5%，2.3%and23.7%, respectively. There was still63.5%of proteinremaining in the residue. The amino acids composition of protein fractions indicated that non polar aminoacids and aromatic amino acid was abundant in glutenin and residual protein. In order to improve theutilization efficiency of protein, defatted Tenebrio molitor (L.) larva was used directly as the raw materialsin the experiments.
Alcalase was chosen to prepare antihypertensive peptides from defatted Tenebrio molitor (L.) larvaprotein. The optimum enzymatic conditions were determinated as follows: substrate concentration3%,Alcalase dosage4000U/g substrate, temperature50℃, pH value8.5. The ACE inhibitory activity was thestrongest when hydrolytic degree reached20%. And the IC50value of the hydrolysates was determined at0.39mg/mL.
Ultrasound (350W/g substrate) was used to treat defatted Tenebrio molitor (L.) larva protein beforeenzymatic hydrolysis in the experiment. The hydrolysis time (DH reached20%) was shorted by20%whenpretreated for10min. The effects of ultrasonic treatment on conformation of Tenebrio molitor (L.) larvaprotein were studied by means of ultraviolet absorption spectra, fluorescence emission spectra, surfacehydrophobicity, free sulfhydryl content, particle size distribution, circular dichroism, and sodium dodecylsulphate-polyacrylamide gel electrophoresis. The results indicated that ultrasonic treatment changed theconformation of albumin and glutenin isolated from defatted Tenebrio molitor (L.) larva. But the primarystructure of protein was not affected by ultrasound.
The effects of ultrasound on the enzymatic hydrolysis of defatted Tenebrio molitor (L.) larva proteinwith Alcalase were also investigated. The results indicated that ultrasonic treatment (2.5and5min) canaccelerate the enzymatic hydrolysis procedures of samples. The influence of ultrasound on activity andconformation of Alcalase was also measured. The result revealed enzyme activity was significantlyimproved as being treated for5min, while extensive processing on the contrary decreased the activity ofAlcalase. The results of ultraviolet absorption and fluorescence emission showed that ultrasonic treatmentled to a change on molecular structure of Alcalase. Amino acid composition in hydrolysates (DH8%) ofTenebrio molitor (L.) larva protein was almost the same whether enzymatic hydrolysis was treated withultrasound or not.
Tenebrio molitor (L.) larva protein hydrolysates was fractionated using Sephadex G-15columnchromatography after decolored by activated carbon, four peaks (Peak1，Peak2，Peak3and Peak4) wereobtained. The results of amino acids composition and relative molecular weight distribution indicated that
Peak2was suitable for production of ACE inhibitory peptides. The IC50value of four fractions isolatedusing gel filtration was determined with high performance liquid chromatography. The value was0.46,0.23,0.83and2.81mg/mL, respectively.
The active fractions in Peak2based on the ACE inhibiting activity were isolated and purified byHPLC. P2-F6and P2-F9among20fractions isolated from Peak2were further purified because of theirstrong ACE inhibitory activity. The amino acid sequences of ACE inhibitory peptides were Ser-Met andTyr-Ala-Asn from P2-F6and Asn-Tyr from P2-F9determined by Matrix-Assisted LaserDesorption/Ionization Time of Flight Mass Spectrometry. The IC50value of them was0.026，0.017and0.011mg/mL, respectively. Ser-Met and Tyr-Ala-Asn have not been reported as antihypertensive peptidesyet.
Blood pressure of spontaneously hypertensive rats (SHR) decreased obviously after fed with thefraction of Peak2, in a single oral administration in100,200and400mg/kg.bw dosage respectively. It isalso discovered that defatted Tenebrio molitor (L.) larva protein hydrolysates has some antioxidant effect.
引文
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