高加索乳杆菌醇脱氢酶的基因克隆、表达及性质研究
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摘要
醇脱氢酶(Alcohol Dehydrogenase, E.C.1.1.1.1.)属于氧化还原酶,在醇类代谢途径中起重要作用,生物体内很多醇类代谢均通过该类酶催化完成。由于醇脱氢酶具有立体专一性还原前手性羰基化合物的能力,因而在氧化还原酶这一大类酶中占有重要地位。醇脱氢酶可用于高效合成具有光学活性的手性醇,后者往往是医药化工业生产用关键结构单元。寻找和开发新的有实用价值的醇脱氢酶并应用于手性药物的生产及其他方面是研究的一大热点。本研究从高加索乳杆菌Lactobacillus kefir DSM20587中克隆了一个新的醇脱氢酶基因LK-adh,进行了重组醇脱氢酶工程菌的构建、表达条件及酶学性质研究,并研究了该酶在不对称还原反应中的对映选择性和辅酶依赖类型,最后对LK-ADH在高加索乳杆菌中的表达进行了初步研究。结果如下:
在生物信息学指导下,结合TAIL-PCR技术从高加索乳杆菌L.kefir DSM20587基因组DNA中克隆得到一个全长1044bp的LK-adh基因。该序列具有完整的开放阅读框,编码347个氨基酸。在GenBank数据库里与已知序列的同源性均不超过78%,该基因已提交GenBank收录,登录号为:EU877965;其编码蛋白的序列登录号为:ACF95832。
将LK-adh基因克隆到表达载体pET-28a(+)上,构建了醇脱氢酶基因工程菌株E.coli BL21(DE3)/pYG461。经IPTG诱导,工程菌株能表达有活性的重组酶。通过培养温度、诱导剂浓度、摇床转速、菌浓和pH值等产酶因素的优化考察,得到工程菌的最佳培养条件为:27℃、pH 6.0、150rpm(偏心距25mm),最佳诱导条件为:OD600达到0.8后用0.2mmol/L IPTG诱导6h。在此条件下酶活2.17×10~(-1)U/ml较优化前的7.2×10~(-2)U/ml提高了201%。
对重组酶进行了纯化与转化产物鉴定的研究,纯化采用包涵体透析复性的方法,纯化后的蛋白经过SDS-PAGE电泳显示为单一条带,比酶活为6.7U/mg,较纯化前提高了3.5倍。LK-ADH能够高对映选择性地转化苯乙酮为(S)-苯乙醇,对映体过量值达到99.4%,同时辅酶依赖类型为NADH型,表明该酶是一种NADH依赖的(S)-醇脱氢酶。
酶学性质研究表明重组醇脱氢酶氧化反应和还原反应的最适反应pH值分别为5.6和5.0;最适反应温度在35℃左右。重组酶在-20℃保藏4周剩余约70%活力;在20~35℃保温1h后活力没有明显的降低。经过动力学参数测定,还原反应:Km=55.37mmol/L;氧化反应:Km=88.60mmol/L。Zn~(2+)及Mg~(2+)对酶活性有促进作用,Cu~(2+)以及还原剂β-巯基乙醇及DTT对LK-ADH的活性有抑制作用。该酶能够有效转化带有较大的侧链基团的酮类化合物如苯乙酮及其衍生物,对各种醇类化合物该酶的氧化反应活性则较低。
通过RT-PCR实验,确认LK-adh基因在L.kefir细胞中呈表达状态,24h转录活性约为12h转录活性的130%;另外在L.kefir中另一种醇脱氢酶基因LK-adh(R)的转录水平在12～24h比LK-adh高38%~63%。此结果证明了在高加索乳杆菌基因组中至少有两种对映选择性相反的醇脱氢酶基因。用L.kefir细胞转化苯乙酮也表明产物包括(R),(S)两种构型的苯乙醇。
Alcohol dehydrogenases (E.C.1.1.1.1, also known as keto-reductase) belong to the class of oxidoreductases. They play an important role in metabolic pathway by catalyzing alcohol metabolism in organism. Among the class of oxidoreductases, alcohol dehydrogenases represent an important group due to their ability to stereospecifically reduce prochiral carbonyl compounds. Alcohol dehydrogenases (ADH) can be used in high-efficient synthesis of optically active alcohols (chiral alcohol), which are key building blocks for the medical and pharmaceutical industry. Finding and developing novel alcohol dehydrogenase applicable in the production of chiral drug or other field is very popular scientific research. In this work, a novel gene named LK-adh encoding alcohol dehydrogenase was cloned from Lactobacillus kefir DSM20587. An engineering strain expressing the recombinant LK-ADH was constructed and the conditions for its expression and enzymology were investigated. The cofactor preference and enantioselectivity of this novel alcohol dehydrogenase in asymmetric reduction were also determined. Finally, a preliminary research was carried out to study the transcription and expression of LK-ADH in Lactobacillus kefir. Details are as follows:
A fragment which consists of an open reading frame (ORF) of 1,044bp, coding for 347 amino acids, was cloned from the genomic DNA of Lactobacillus kefir DSM20587 with the help of bioinformatics and TAIL-PCR. The ORF was analyzed and named as LK-adh by a Blast similarity search in GenBank database. The highest homology was found less than 78% at protein level. This novel gene was deposited into GenBank with the accession number of EU877965 and the corresponding protein sequence could be found under the accession number of ACF95832.
LK-adh was then subcloned into the plasmid pET-28a(+) followed by transforming into E.coli BL21(DE3) to obtain the engineering strain E.coli BL21(DE3)/pYG461. The recombinant LK-ADH could be efficiently expressed by IPTG induction. The conditions for enzyme activity such as incubation temperature, IPTG concentration, rotation speed of shaker and so on were studied.The optimum conditions for incubation of engineering strain were as follows:temperature 27℃,initial pH value of medium 6.0, rotation speed of shaker 150rpm; the optimum conditions for the induction of recombinant LK-ADH were:optical density of engineering strain (OD600) 0.8, 0.2mmol/L IPTG,induction time 6 h. Under these conditions, the recombinant enzyme activity was increased from 7.2×10~(-2)U/ml to 2.17×10~(-1)U/ml.
The recombinant LK-ADH was purified to apparent homogeneity in SDS-PAGE and the purification factor was 4.5 fold while the specific activity of the purified enzyme was 6.7 U/mg. LK-ADH showed high enantioselectivity in the reduction of acetophenone to (S)-phenylethanol, the enantiomeric excess (ee) value was calculated as 99.4%. Coenzyme dependent assay indicated that NADH was preferably used as a cofactor. Therefore, LK-ADH was identified to be a NADH-dependent (S)-specific alcohol dehydrogenase.
The zymological properties of recombinant enzyme were characterized. The optimum pH in oxidative and reductive reaction is 5.6 and 5.0 respectively and the optimum reaction temperature is 35℃. The enzyme activity had no obvious loss after stored at 20~35℃for 1h . However, only 70% activity was remained if stored at -20℃for 4 weeks. The Km values of the LK-ADH in reductive and oxidative reaction were 55.37mmol/L and 88.60mmol/L respectively. The enzyme activity could be activated by Zn~(2+) and Mg~(2+), but inhibited by Cu~(2+), 2-mercaptoethanol and DTT. LK-ADH showed relatively high activity with all the tested aldehydes as substrates but low activity in oxidation of alcohols. Ketones with bulky side chains, such as acetophenone and its derivative were also found to be effectively transformed to their corresponding alcohols. .
LK-adh was identified to be continuously expressed in L.kefir cell by RT-PCR analysis. The transcription level at 24h was 130% as compared with that at 12h, however, 38%~63% lower than those by a previously reported alcohol dehydrogenase gene LK-adh(R) in L.kefir cell at 12h and 24h. These results showed that at least two alcohol dehydrogenase genes with different enantioselectivity are existed in the genome of Lactobacillus kefir. Transformation of acetophenone by L.kefir cell also showed that both (R) and (S)-phenylethanol were acquired in the products.
在生物信息学指导下,结合TAIL-PCR技术从高加索乳杆菌L.kefir DSM20587基因组DNA中克隆得到一个全长1044bp的LK-adh基因。该序列具有完整的开放阅读框,编码347个氨基酸。在GenBank数据库里与已知序列的同源性均不超过78%,该基因已提交GenBank收录,登录号为:EU877965;其编码蛋白的序列登录号为:ACF95832。
将LK-adh基因克隆到表达载体pET-28a(+)上,构建了醇脱氢酶基因工程菌株E.coli BL21(DE3)/pYG461。经IPTG诱导,工程菌株能表达有活性的重组酶。通过培养温度、诱导剂浓度、摇床转速、菌浓和pH值等产酶因素的优化考察,得到工程菌的最佳培养条件为:27℃、pH 6.0、150rpm(偏心距25mm),最佳诱导条件为:OD600达到0.8后用0.2mmol/L IPTG诱导6h。在此条件下酶活2.17×10~(-1)U/ml较优化前的7.2×10~(-2)U/ml提高了201%。
对重组酶进行了纯化与转化产物鉴定的研究,纯化采用包涵体透析复性的方法,纯化后的蛋白经过SDS-PAGE电泳显示为单一条带,比酶活为6.7U/mg,较纯化前提高了3.5倍。LK-ADH能够高对映选择性地转化苯乙酮为(S)-苯乙醇,对映体过量值达到99.4%,同时辅酶依赖类型为NADH型,表明该酶是一种NADH依赖的(S)-醇脱氢酶。
酶学性质研究表明重组醇脱氢酶氧化反应和还原反应的最适反应pH值分别为5.6和5.0;最适反应温度在35℃左右。重组酶在-20℃保藏4周剩余约70%活力;在20~35℃保温1h后活力没有明显的降低。经过动力学参数测定,还原反应:Km=55.37mmol/L;氧化反应:Km=88.60mmol/L。Zn~(2+)及Mg~(2+)对酶活性有促进作用,Cu~(2+)以及还原剂β-巯基乙醇及DTT对LK-ADH的活性有抑制作用。该酶能够有效转化带有较大的侧链基团的酮类化合物如苯乙酮及其衍生物,对各种醇类化合物该酶的氧化反应活性则较低。
通过RT-PCR实验,确认LK-adh基因在L.kefir细胞中呈表达状态,24h转录活性约为12h转录活性的130%;另外在L.kefir中另一种醇脱氢酶基因LK-adh(R)的转录水平在12～24h比LK-adh高38%~63%。此结果证明了在高加索乳杆菌基因组中至少有两种对映选择性相反的醇脱氢酶基因。用L.kefir细胞转化苯乙酮也表明产物包括(R),(S)两种构型的苯乙醇。
Alcohol dehydrogenases (E.C.1.1.1.1, also known as keto-reductase) belong to the class of oxidoreductases. They play an important role in metabolic pathway by catalyzing alcohol metabolism in organism. Among the class of oxidoreductases, alcohol dehydrogenases represent an important group due to their ability to stereospecifically reduce prochiral carbonyl compounds. Alcohol dehydrogenases (ADH) can be used in high-efficient synthesis of optically active alcohols (chiral alcohol), which are key building blocks for the medical and pharmaceutical industry. Finding and developing novel alcohol dehydrogenase applicable in the production of chiral drug or other field is very popular scientific research. In this work, a novel gene named LK-adh encoding alcohol dehydrogenase was cloned from Lactobacillus kefir DSM20587. An engineering strain expressing the recombinant LK-ADH was constructed and the conditions for its expression and enzymology were investigated. The cofactor preference and enantioselectivity of this novel alcohol dehydrogenase in asymmetric reduction were also determined. Finally, a preliminary research was carried out to study the transcription and expression of LK-ADH in Lactobacillus kefir. Details are as follows:
A fragment which consists of an open reading frame (ORF) of 1,044bp, coding for 347 amino acids, was cloned from the genomic DNA of Lactobacillus kefir DSM20587 with the help of bioinformatics and TAIL-PCR. The ORF was analyzed and named as LK-adh by a Blast similarity search in GenBank database. The highest homology was found less than 78% at protein level. This novel gene was deposited into GenBank with the accession number of EU877965 and the corresponding protein sequence could be found under the accession number of ACF95832.
LK-adh was then subcloned into the plasmid pET-28a(+) followed by transforming into E.coli BL21(DE3) to obtain the engineering strain E.coli BL21(DE3)/pYG461. The recombinant LK-ADH could be efficiently expressed by IPTG induction. The conditions for enzyme activity such as incubation temperature, IPTG concentration, rotation speed of shaker and so on were studied.The optimum conditions for incubation of engineering strain were as follows:temperature 27℃,initial pH value of medium 6.0, rotation speed of shaker 150rpm; the optimum conditions for the induction of recombinant LK-ADH were:optical density of engineering strain (OD600) 0.8, 0.2mmol/L IPTG,induction time 6 h. Under these conditions, the recombinant enzyme activity was increased from 7.2×10~(-2)U/ml to 2.17×10~(-1)U/ml.
The recombinant LK-ADH was purified to apparent homogeneity in SDS-PAGE and the purification factor was 4.5 fold while the specific activity of the purified enzyme was 6.7 U/mg. LK-ADH showed high enantioselectivity in the reduction of acetophenone to (S)-phenylethanol, the enantiomeric excess (ee) value was calculated as 99.4%. Coenzyme dependent assay indicated that NADH was preferably used as a cofactor. Therefore, LK-ADH was identified to be a NADH-dependent (S)-specific alcohol dehydrogenase.
The zymological properties of recombinant enzyme were characterized. The optimum pH in oxidative and reductive reaction is 5.6 and 5.0 respectively and the optimum reaction temperature is 35℃. The enzyme activity had no obvious loss after stored at 20~35℃for 1h . However, only 70% activity was remained if stored at -20℃for 4 weeks. The Km values of the LK-ADH in reductive and oxidative reaction were 55.37mmol/L and 88.60mmol/L respectively. The enzyme activity could be activated by Zn~(2+) and Mg~(2+), but inhibited by Cu~(2+), 2-mercaptoethanol and DTT. LK-ADH showed relatively high activity with all the tested aldehydes as substrates but low activity in oxidation of alcohols. Ketones with bulky side chains, such as acetophenone and its derivative were also found to be effectively transformed to their corresponding alcohols. .
LK-adh was identified to be continuously expressed in L.kefir cell by RT-PCR analysis. The transcription level at 24h was 130% as compared with that at 12h, however, 38%~63% lower than those by a previously reported alcohol dehydrogenase gene LK-adh(R) in L.kefir cell at 12h and 24h. These results showed that at least two alcohol dehydrogenase genes with different enantioselectivity are existed in the genome of Lactobacillus kefir. Transformation of acetophenone by L.kefir cell also showed that both (R) and (S)-phenylethanol were acquired in the products.
引文
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