WEKO3
アイテム
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Escherichia coli K-12由来のイソアスパラギナーゼ遺伝子(pepE)のクローニングと大量発現
https://pu-toyama.repo.nii.ac.jp/records/224
https://pu-toyama.repo.nii.ac.jp/records/224b1da1ad5-42c6-4d87-9e67-584ac31c25cb
名前 / ファイル | ライセンス | アクション |
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KJ00004182044.pdf (562.0 kB)
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Item type | [ELS]紀要論文 / Departmental Bulletin Paper(1) | |||||
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公開日 | 2017-02-24 | |||||
タイトル | ||||||
タイトル | Escherichia coli K-12由来のイソアスパラギナーゼ遺伝子(pepE)のクローニングと大量発現 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Cloning of isoasparaginase (αaspartyl dipeptidase) gene from Escherichia coli K-12 and overexpression of the gene in E. coli | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | アスパルテーム | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | イソアスパラギナーゼ | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | α-アスパルチルジペプチダーゼ(PepE) | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Escherichia coli | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Aspartame | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | isoasparaginase | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | α-aspartlyl dipeptidase | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | pepE | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Escherichia coli | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | departmental bulletin paper | |||||
雑誌書誌ID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AN10358595 | |||||
著者 |
米田, 英伸
× 米田, 英伸× 水口, 直之× 吉良, 郁夫× 横関, 健三× 浅野, 泰久× KOMEDA, Hidenobu× MIZUGUCHI, Naoyuki× KIRA, Ikuo× YOKOZEKI, Kenzo× ASANO, Yasuhisa |
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著者所属(日) | ||||||
値 | 富山県立大学生物工学研究センター | |||||
著者所属(日) | ||||||
値 | 富山県立大学生物工学研究センター | |||||
著者所属(日) | ||||||
値 | 富山県立大学生物工学研究センター | |||||
著者所属(日) | ||||||
値 | 味の素(株) | |||||
著者所属(日) | ||||||
値 | 富山県立大学生物工学研究センター | |||||
著者所属(英) | ||||||
言語 | en | |||||
値 | Biotechnology Reseach Center | |||||
著者所属(英) | ||||||
言語 | en | |||||
値 | Biotechnology Reseach Center | |||||
著者所属(英) | ||||||
言語 | en | |||||
値 | Biotechnology Reseach Center | |||||
著者所属(英) | ||||||
言語 | en | |||||
値 | Ajinomoto Co. Ltd. / | |||||
抄録(日) | ||||||
内容記述タイプ | Other | |||||
内容記述 | L-イソアスパラギンのα-アミド基を加水分解し、アスパラギン酸を生成する反応を触媒するイソアスパラギナーゼと同一酵素と考えられるα-アスパルチルジペプチターゼ(pepE)をコードする遺伝子、pepEを大腸菌K-12株よりクローン化した。その開始コドン上流部分を改良したpepEを大腸菌JM109株で大量発現させた場合、その無細胞抽出液のPepE活性はL-アスパラギンサンP-ニトロアニリドを基質とした場合、2.92ユニット/ミリグラムとなった。この値はコントロールの2100倍である。本酵素を大腸菌形質転換体の無細胞抽出液より精製し、その酵素化学的諸性質を明らかにした。本酵素は50℃及びpH8.0において最大活性を示した。精製酵素を用いてL-イソアスパラギンとL-フェニルアラニンメチルエステルからのアスパルテームの合成を検討した。 | |||||
抄録(英) | ||||||
内容記述タイプ | Other | |||||
内容記述 | Isoasparaginase from E. coli K-12, which catalyzes the hydrolysis of L-isoastaragine to form L-aspartic acid and ammonia, was previously identified as α-aspartyl dipeptidase. The gene encoding the isoasparaginase (α-aspartyl depeptidase, PepE) was colned from the chromosomal DNA of E. coli K-12. The pepE gene modified in the nucleotide sequence upstream from its start codon was overespressed in E. coli JM109. The activity of the recombinant PepE enzyme in cell-free extracts of E. coli JM109 harboring pepE-expression plasmid was 2.92 units mg_-1 with L-aspartic acid p-nitoroanilide as substrate, which was 2100 times higher than that of E.coli hast. This enzyme was purified to electrophoretic homogeneity by ammonium sulfate fractionation and four column chromatography steps. It had maximal activity at 50℃ and pH 8.0. Enzymatic synthesis of aspartame was attempted using the purified PepE with L-isoasparagine and L-phenylalanine methyl ester as substrates. | |||||
書誌情報 |
富山県立大学紀要 en : Bulletin of Toyama Prefectural University 巻 15, p. 91-96, 発行日 2005-03-31 |
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表示順 | ||||||
内容記述タイプ | Other | |||||
内容記述 | 15 | |||||
アクセション番号 | ||||||
内容記述タイプ | Other | |||||
内容記述 | KJ00004182044 | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 09167633 |