太平洋磷虾（Euphausia pacifica Hansen）胰蛋白酶样酶酶学性质及基因片段研究
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摘要
本文通过分离纯化太平洋磷虾胰蛋白酶样酶,对其相关的酶学性质进行研究。并克隆其基因进行序列分析,探讨其酶学性质的分子机理。以期为胰蛋白酶样酶的理论研究及其医学、工业应用提供理论基础。
采用双向电泳及生物大分子质谱技术,在太平洋磷虾粗酶液内鉴定到至少两种胰蛋白酶样酶。太平洋磷虾粗酶液经35~65 %饱和度硫酸铵分级沉淀,DEAE Sepharose Fast Flow离子交换层析, Sephadex G100凝胶过滤层析以及Benzamidine Sepharose 4B亲和层析得到两种胰蛋白酶样酶,TLE I和TLE II,相对分子量分别为32.9和32.3 kDa。TLE I比活力为91.4 BApNA单位每毫克蛋白,纯化倍数为177;TLE II比活力为113 BApNA单位每毫克蛋白,纯化倍数为218。两种胰蛋白酶样酶促反应的速率受pH、温度影响。在37°C,以BApNA为底物的反应体系中,两种酶在较广泛的pH范围(6.0~11.0)内具有较高活性,反应最适宜pH在9.0~10.0之间;在pH 9.0,以BApNA为底物的反应体系中,两种酶在较广泛的温度范围(20~70°C)内具有较高活性,反应最适宜温度为40 ~50°C。两种胰蛋白酶样酶在低于40°C温度范围内保持稳定,在高于40°C时稳定性降低。
Mg2+(≥0.3 mmol L-1)和Ca2+(≥0.2 mmol L-1)对两种胰蛋白酶样酶有一定的激活作用,Zn2+(≥0.1 mmol L-1)、Cu2+(≥0.2 mmol L-1)、Pb2+(≥0.1 mmol L-1)、Hg2+(≥0.1 mmol L-1)对两种酶均有一定抑制作用,其中Pb2+和Hg2+对两种酶表现出强烈的抑制。
乙醇(≤10 %)、丙三醇(≤5 %)和二甲亚砜(≤5 %)在低浓度时对两种胰蛋白酶样酶活性无明显影响,高浓度(分别为≥15 %、≥10 %、≥10 %)下表现为强烈抑制作用;丙酮(≥5 %)对两种酶有较强烈的抑制作用。
丝氨酸蛋白酶专一性抑制剂苯甲基磺酰氟(PMSF)、大豆胰蛋白酶抑制剂(STI)以及胰蛋白酶专一性抑制剂对氨基苯甲脒(p-amionbenzamidine)、鸡卵类粘蛋白(CEOM)、苯甲脒(benzamidine)、N-对甲苯磺酰-L-赖氨酸氯甲酮(TLCK)对两种胰蛋白酶样酶具不同程度抑制作用,胰凝乳蛋白酶专一性抑制剂N-对甲苯磺酰-L-苯丙氨酸氯甲酮(TPCK)对两种胰蛋白酶样酶无抑制作用。证明这两种酶是胰蛋白酶,属于丝氨酸蛋白酶家族。
TLE I的米氏常数Km= 0.088 mmol L-1;催化常数(转换数)Kcat=0.84 S-1;表观二级速率常数(专一性常数,转换效率)Kcat / Km =9.54 mmol L-1 S-1;TLE II的Km=0.064 mmol L-1;催化常数(转换数)Kcat=0.98 S-1;表观二级速率常数(专一性常数,转换效率)Kcat / Km =15.3 mmol L-1 S-1。TLE的Kcat/Km较某些生物胰蛋白酶高1.6~6.7倍。
Benzamidine对TLE I抑制类型为非竞争性抑制,抑制剂常数Ki=0.07 mmol L-1。
组氨酸残基、色氨酸残基是构成TLE I酶活性中心的必需基团。精氨酸残基可能是该酶活性中心结合部位的关键基团。赖氨酸的游离ε-氨基与酶活性有关,巯基可能与酶活性相关。游离羧基不是TLE I活性中心的必需功能基团。
太平洋磷虾、南极大磷虾、中国毛虾、中国明对虾、刀额新对虾、脊尾白虾、日本蟳、三疣梭子蟹、中华绒螯蟹等九种甲壳动物胰蛋白酶基因基因结构基本一致。在同一物种内,至少有三个基因家族,各家族间第二个内含子有13.2~66.1 %相似度,基因间有65.9~90 %相似度;各家族内部的第二个内含子有1.9~6.2 %的变异,基因间有2.5~6.7 %变异。
动物胰蛋白酶接触反应三联体是保守的,底物结合位点Asp、盐键形成位点Asp以及二硫键形成位点(昆虫缺失两个)在绝大多数物种中也较保守,形成4个二硫键(昆虫只有3个)。
系统进化树分析表明物种进化过程中,胰蛋白酶基因分化与演进过程可能与物种分化与演进的过程并不完全一致。
甲壳动物胰蛋白酶极性氨基酸如精氨酸含量较低,Arg/(Arg+Lys)比值较低,天冬氨酸、谷氨酸含量较高;非极性氨基酸如异亮氨酸含量较高,而甲硫氨酸、脯氨酸含量较低。这些可能也是甲壳动物对环境理化因子及饵料成分、丰度多变的一种适应。在上述条件下甲壳动物演化出pH、温度稳定性较低但是柔性较高、降解效率较高的胰蛋白酶。
In this paper, trypsin-like enzymes (TLEs) were purified from North Pacific krill (Euphausia pacifica Hansen) and characterized. Trypsin genes were cloned, sequenced and analysised. This is aimed to provide primary data and theory support for future commercial utilization of E. pacifica TLEs in science, medicine and industry.
At least two TLEs were identified from the crude exact of E. pacifica by 2 dimensional electrophoresis (2-DE) and mass spectrometry (MS). By solid ammonium sulfate fractional precipitation with saturation between 35 % and 65 %, DEAE sepharose Fast Flow ion exchange chromatography, sephadex G100 gel chromatography and Benzamidine Sepharose 4B affinity chromatography, two TLEs, TLE I and TLE II were purified. They had molecular masses of 32.9 and 32.3 kDa respectively. The specific activity and purification fold of TLE I were 91.4 BApNA Unit per mg protein and 177. And those of TLE II were 113 BApNA Unit per mg protein and 218 respectively.
The purified TLE I and TLE II were active in extremely wide pH range of 6.0~11.0 and the optimum values were between pH 9.0 and 10.0 at 37°C with BApNA as subtrate. And they were active in temperature range of 20~70°C, extremely wide, with optimum values between 40 and 50°C at pH 9.0, BApNA as subtrate. TLE I and TLE II were stable at 40°C or lower, which were deactivated with temperature over 40°C。
With metal ions, Mg2+(≥0.3 mmol L-1)and Ca2+(≥0.2 mmol L-1) had activation on TLE I and TLE II, while Zn2+(≥0.1 mmol L-1), Cu2+(≥0.2 mmol L-1), Hg2+(≥0.1 mmol L-1) and Pb2+(≥0.1 mmol L-1)showed different degree of inhibition on them, especially obvious at the presence of Hg2+ and Pb2+.
The activities of TLE I and TLE II were relative stable with ethanol (≤10 %), glycerin (≤5 %) and Dimethyl sulphoxide (DMSO) (≤5 %) and deactivated with concentration over≥15 %,≥10 %,≥10 %10 % (v/v) respectively. Inhibitions of acetone (≥5 %) were significantly.
Serine specific inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and soybean trypsin inhibotor (STI), and trypsin specific inhibitors, such as p-amionbenzamidine, chicken egg ovomucoid (CEOM), benzamidine and N-α-tysol-L-lysine chloromethyl ketone (TLCK) had different degree of inhibition on TLE I and TLE II; chymotrypsin specific inhibitor, N-α-tysol-L-phenylalanine chloromethyl ketone had no inhibition on TLE I and TLE II. It confirmed that TLE I and TLE II were of trypsins and belonged to serine proteinase families. The Km, Kcat and Kcat / Km of TLE I was 0.088 mmol L-1, 0.84 S-1 and 9.54 mmol L-1 S-1. And those of TLE II was 0.064 mmol L-1, 0.98 S-1and 15.3 mmol L-1 S-1 respectively。The Kcat / Km of the TLEs were 1.6~6.7 times higher than other organism.
The inhibition type of Benzamidine on TLE I is noncompetitive inhibition, and the inhibitor constant of Benzamidine is 0.07 mmol L-1.
The functional group study of TLE I showed that, tryptophan residue and histidine residue is essential group to active center. And it was speculated the arginine residue might be an essential group to active center. The freeε-amino group of lysinethe residue had relation with enzyme activity and the free hydroxyl group might have relation with it. According to the result, sulfhydryl group had no relation with enzyme active centre.
Study on trypsin gene of 9 kinds of crustaceans revealed the consistence of gene structure in them. There are at least three trypsin gene families, with 13.2~66.1 % identity between introns and 65.9~90 % identity between genes of different families; and 1.9~6.2 % mutation between introns and 2.5~6.7 % mutation between genes of the same families.
Analysis on the sequence of deduced protein showed that the essential active center, such as the catalytic triad residues, substrate binding group and disulfide bridge were conservative in crustaceans.
The evolution rule revealed by polygenetic analysis on trypsin amino acids sequence might do not consistent with evolution theory nowadays completely.
It was speculated that, because of low content of polar amino acid, such as Arg, Lys and Arg/(Arg+Lys) ratio, high Asp, Glu and Ile content, low Met and Pro content in crustacean trypsins, they had lower pH-thermal stability, but higher flexibility, especially higher physiological efficiency with them.
采用双向电泳及生物大分子质谱技术,在太平洋磷虾粗酶液内鉴定到至少两种胰蛋白酶样酶。太平洋磷虾粗酶液经35~65 %饱和度硫酸铵分级沉淀,DEAE Sepharose Fast Flow离子交换层析, Sephadex G100凝胶过滤层析以及Benzamidine Sepharose 4B亲和层析得到两种胰蛋白酶样酶,TLE I和TLE II,相对分子量分别为32.9和32.3 kDa。TLE I比活力为91.4 BApNA单位每毫克蛋白,纯化倍数为177;TLE II比活力为113 BApNA单位每毫克蛋白,纯化倍数为218。两种胰蛋白酶样酶促反应的速率受pH、温度影响。在37°C,以BApNA为底物的反应体系中,两种酶在较广泛的pH范围(6.0~11.0)内具有较高活性,反应最适宜pH在9.0~10.0之间;在pH 9.0,以BApNA为底物的反应体系中,两种酶在较广泛的温度范围(20~70°C)内具有较高活性,反应最适宜温度为40 ~50°C。两种胰蛋白酶样酶在低于40°C温度范围内保持稳定,在高于40°C时稳定性降低。
Mg2+(≥0.3 mmol L-1)和Ca2+(≥0.2 mmol L-1)对两种胰蛋白酶样酶有一定的激活作用,Zn2+(≥0.1 mmol L-1)、Cu2+(≥0.2 mmol L-1)、Pb2+(≥0.1 mmol L-1)、Hg2+(≥0.1 mmol L-1)对两种酶均有一定抑制作用,其中Pb2+和Hg2+对两种酶表现出强烈的抑制。
乙醇(≤10 %)、丙三醇(≤5 %)和二甲亚砜(≤5 %)在低浓度时对两种胰蛋白酶样酶活性无明显影响,高浓度(分别为≥15 %、≥10 %、≥10 %)下表现为强烈抑制作用;丙酮(≥5 %)对两种酶有较强烈的抑制作用。
丝氨酸蛋白酶专一性抑制剂苯甲基磺酰氟(PMSF)、大豆胰蛋白酶抑制剂(STI)以及胰蛋白酶专一性抑制剂对氨基苯甲脒(p-amionbenzamidine)、鸡卵类粘蛋白(CEOM)、苯甲脒(benzamidine)、N-对甲苯磺酰-L-赖氨酸氯甲酮(TLCK)对两种胰蛋白酶样酶具不同程度抑制作用,胰凝乳蛋白酶专一性抑制剂N-对甲苯磺酰-L-苯丙氨酸氯甲酮(TPCK)对两种胰蛋白酶样酶无抑制作用。证明这两种酶是胰蛋白酶,属于丝氨酸蛋白酶家族。
TLE I的米氏常数Km= 0.088 mmol L-1;催化常数(转换数)Kcat=0.84 S-1;表观二级速率常数(专一性常数,转换效率)Kcat / Km =9.54 mmol L-1 S-1;TLE II的Km=0.064 mmol L-1;催化常数(转换数)Kcat=0.98 S-1;表观二级速率常数(专一性常数,转换效率)Kcat / Km =15.3 mmol L-1 S-1。TLE的Kcat/Km较某些生物胰蛋白酶高1.6~6.7倍。
Benzamidine对TLE I抑制类型为非竞争性抑制,抑制剂常数Ki=0.07 mmol L-1。
组氨酸残基、色氨酸残基是构成TLE I酶活性中心的必需基团。精氨酸残基可能是该酶活性中心结合部位的关键基团。赖氨酸的游离ε-氨基与酶活性有关,巯基可能与酶活性相关。游离羧基不是TLE I活性中心的必需功能基团。
太平洋磷虾、南极大磷虾、中国毛虾、中国明对虾、刀额新对虾、脊尾白虾、日本蟳、三疣梭子蟹、中华绒螯蟹等九种甲壳动物胰蛋白酶基因基因结构基本一致。在同一物种内,至少有三个基因家族,各家族间第二个内含子有13.2~66.1 %相似度,基因间有65.9~90 %相似度;各家族内部的第二个内含子有1.9~6.2 %的变异,基因间有2.5~6.7 %变异。
动物胰蛋白酶接触反应三联体是保守的,底物结合位点Asp、盐键形成位点Asp以及二硫键形成位点(昆虫缺失两个)在绝大多数物种中也较保守,形成4个二硫键(昆虫只有3个)。
系统进化树分析表明物种进化过程中,胰蛋白酶基因分化与演进过程可能与物种分化与演进的过程并不完全一致。
甲壳动物胰蛋白酶极性氨基酸如精氨酸含量较低,Arg/(Arg+Lys)比值较低,天冬氨酸、谷氨酸含量较高;非极性氨基酸如异亮氨酸含量较高,而甲硫氨酸、脯氨酸含量较低。这些可能也是甲壳动物对环境理化因子及饵料成分、丰度多变的一种适应。在上述条件下甲壳动物演化出pH、温度稳定性较低但是柔性较高、降解效率较高的胰蛋白酶。
In this paper, trypsin-like enzymes (TLEs) were purified from North Pacific krill (Euphausia pacifica Hansen) and characterized. Trypsin genes were cloned, sequenced and analysised. This is aimed to provide primary data and theory support for future commercial utilization of E. pacifica TLEs in science, medicine and industry.
At least two TLEs were identified from the crude exact of E. pacifica by 2 dimensional electrophoresis (2-DE) and mass spectrometry (MS). By solid ammonium sulfate fractional precipitation with saturation between 35 % and 65 %, DEAE sepharose Fast Flow ion exchange chromatography, sephadex G100 gel chromatography and Benzamidine Sepharose 4B affinity chromatography, two TLEs, TLE I and TLE II were purified. They had molecular masses of 32.9 and 32.3 kDa respectively. The specific activity and purification fold of TLE I were 91.4 BApNA Unit per mg protein and 177. And those of TLE II were 113 BApNA Unit per mg protein and 218 respectively.
The purified TLE I and TLE II were active in extremely wide pH range of 6.0~11.0 and the optimum values were between pH 9.0 and 10.0 at 37°C with BApNA as subtrate. And they were active in temperature range of 20~70°C, extremely wide, with optimum values between 40 and 50°C at pH 9.0, BApNA as subtrate. TLE I and TLE II were stable at 40°C or lower, which were deactivated with temperature over 40°C。
With metal ions, Mg2+(≥0.3 mmol L-1)and Ca2+(≥0.2 mmol L-1) had activation on TLE I and TLE II, while Zn2+(≥0.1 mmol L-1), Cu2+(≥0.2 mmol L-1), Hg2+(≥0.1 mmol L-1) and Pb2+(≥0.1 mmol L-1)showed different degree of inhibition on them, especially obvious at the presence of Hg2+ and Pb2+.
The activities of TLE I and TLE II were relative stable with ethanol (≤10 %), glycerin (≤5 %) and Dimethyl sulphoxide (DMSO) (≤5 %) and deactivated with concentration over≥15 %,≥10 %,≥10 %10 % (v/v) respectively. Inhibitions of acetone (≥5 %) were significantly.
Serine specific inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and soybean trypsin inhibotor (STI), and trypsin specific inhibitors, such as p-amionbenzamidine, chicken egg ovomucoid (CEOM), benzamidine and N-α-tysol-L-lysine chloromethyl ketone (TLCK) had different degree of inhibition on TLE I and TLE II; chymotrypsin specific inhibitor, N-α-tysol-L-phenylalanine chloromethyl ketone had no inhibition on TLE I and TLE II. It confirmed that TLE I and TLE II were of trypsins and belonged to serine proteinase families. The Km, Kcat and Kcat / Km of TLE I was 0.088 mmol L-1, 0.84 S-1 and 9.54 mmol L-1 S-1. And those of TLE II was 0.064 mmol L-1, 0.98 S-1and 15.3 mmol L-1 S-1 respectively。The Kcat / Km of the TLEs were 1.6~6.7 times higher than other organism.
The inhibition type of Benzamidine on TLE I is noncompetitive inhibition, and the inhibitor constant of Benzamidine is 0.07 mmol L-1.
The functional group study of TLE I showed that, tryptophan residue and histidine residue is essential group to active center. And it was speculated the arginine residue might be an essential group to active center. The freeε-amino group of lysinethe residue had relation with enzyme activity and the free hydroxyl group might have relation with it. According to the result, sulfhydryl group had no relation with enzyme active centre.
Study on trypsin gene of 9 kinds of crustaceans revealed the consistence of gene structure in them. There are at least three trypsin gene families, with 13.2~66.1 % identity between introns and 65.9~90 % identity between genes of different families; and 1.9~6.2 % mutation between introns and 2.5~6.7 % mutation between genes of the same families.
Analysis on the sequence of deduced protein showed that the essential active center, such as the catalytic triad residues, substrate binding group and disulfide bridge were conservative in crustaceans.
The evolution rule revealed by polygenetic analysis on trypsin amino acids sequence might do not consistent with evolution theory nowadays completely.
It was speculated that, because of low content of polar amino acid, such as Arg, Lys and Arg/(Arg+Lys) ratio, high Asp, Glu and Ile content, low Met and Pro content in crustacean trypsins, they had lower pH-thermal stability, but higher flexibility, especially higher physiological efficiency with them.
引文
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