文献一覧: 公益社団法人日本生物工学会 (出版者)

1 0 0 0 根っこのマトリョーシカ

著者: 橋床泰之
出版者: 公益社団法人日本生物工学会
雑誌: 生物工学会誌 : seibutsu-kogaku kaishi (ISSN:09193758)
巻号頁・発行日: vol.81, no.10, 2003-10-25

2022-03-29 18:45:07
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https://ci.nii.ac.jp/naid/110002913009

1 0 0 0 高分子化補酵素の合成とその酵素リアクターへの応用

著者: 卜部格
出版者: 公益社団法人日本生物工学会
雑誌: 醗酵工学会誌 : hakkokogaku kaishi (ISSN:03856151)
巻号頁・発行日: vol.64, no.2, pp.77-97, 1986-03-25

1. An NAD derivative carrying a vinyl group was copolymerized with acrylamide or methacrylamide, and various water-soluble macromolecular NAD derivatives (polymeric NAD derivatives) were obtained. I investigated the coenzymic properties of the polymeric NAD derivatives and concluded that smaller NAD derivatives and lower NAD contents in the polymer chain had higher cofactor activity.2. Poly(ethylene glycol)-bound NAD (PEG-NAD) was prepared by coupling N^6-(2-carboxyethyl)-NAD to one termial of α, ω-diaminopoly(etylene glycol) with water-soluble carbodiimide. The kinetic properties of NAD(H), N^6-(2-carboxyethyl)-NAD(H) and PEG-NAD(H) were investigated with various dehydrogenases from different sources.3. NADP derivatives alkylated at the 2'-phosphate and/or 6-amino groups of the adenosyl moiety were prepared, and the effects of these modifications of NADP on its cofactor activity for various dehydrogenases were investigated. Then, poly(ethylene glycol)-bound NADP (PEG-NADP) was prepared by selective alkylation of the 6-amino group of NAD. PEG-NADP has good cofactor activity for some dehydrogenases but not for isocitrate or glucose dehydrogenases.4. The kinetic properties of a continuous enzyme reactor containing rabbit muscle lactate dehydrogenase, horse liver alcohol dehydrogenase, and PEG-NAD were investigated experimentally and theoretically. The steady-state behavior of the enzyme reactor was explained semi-quantitatively by a simple kinetic model. The operational stability of a continuous enzyme reactor containing PEG-NAD and thermostable dehydrogenases was also studied.

2021-12-20 02:17:01
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https://ci.nii.ac.jp/naid/110002777892

1 0 0 0 システム論的アプローチによる複合微生物系の解析と制御(「環境」と生物工学,<特集>バイオ技術10年の軌跡,創立90周年記念特別企画)

著者: 松本慎也常田聡
出版者: 公益社団法人日本生物工学会
雑誌: 生物工学会誌 : seibutsu-kogaku kaishi (ISSN:09193758)
巻号頁・発行日: vol.90, no.4, pp.160-164, 2012-04-25

2021-12-13 05:04:32
1 + 2 Wikipedia

https://ci.nii.ac.jp/naid/110009445709

1 0 0 0 ブルーデキストラン-セファロースアフィニティクロマトグラフィーによるLactobacillus buchneriグルコース-6-リン酸脱水素酵素の精製

著者: 河合啓一江口良友
出版者: 公益社団法人日本生物工学会
雑誌: 醗酵工學雑誌 (ISSN:03675963)
巻号頁・発行日: vol.54, no.2, pp.128-130, 1976-02-25

Lactobacillus buchneri IFO 3961の無細胞抽出液より, グルコース-6-リン酸脱水素酵素をブルーデキストラン-セファロース4Bを用いたアファニティクロマトグラフィーにより精製した.本酵素は低イオン強度条件下に.ブルーデキストラン-セフィロースに吸着され, 1mM NADPあるいは1M塩化カリウムを含む10mMリン酸カリウム緩衝液(pH7)にてほぼ定量的に溶出された.塩化カリウムを用いる直線的濃度勾配法により溶出したところ, 約80%の収率で比活性約120倍の酵素標品を得ることが出来た.本標品はpH9.4でのポリアクリルアミドゲルデイスク電気泳動により単一のバンドを示した.

2021-11-25 20:15:05
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https://ci.nii.ac.jp/naid/110002856928

1 0 0 0 202 ファジィ理論を用いた微生物反応系の異常診断

著者: 淺間一ポッキネンマリウットブスタマンテソイラ長棟輝行遠藤勲多久和正平田彰
出版者: 公益社団法人日本生物工学会
雑誌: 日本醗酵工学会大会講演要旨集
巻号頁・発行日: vol.2, 1990-10-10

2021-11-11 10:30:05
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https://ci.nii.ac.jp/naid/110002904266

1 0 0 0 赤ワインのマロラクチック発酵におけるL-, D-乳酸の生成

著者: 原昌道水野昭博
出版者: 公益社団法人日本生物工学会
雑誌: 醗酵工学会誌 : hakkokogaku kaishi (ISSN:03856151)
巻号頁・発行日: vol.59, no.1, pp.17-22, 1981-01-25
被引用文献数: 1

Most of the lactate formed by malo-lactic fermentation (MLF) during storage of the red wines produced at our Institute was the L(+)-isomer. From these MLF wines, a malo-lactic bacterium which produced mainly D-lactate from glucose by lactic acid fermentation was isolated and classified as Leuconostoc mesenteroides. The production of L-or D-lactate from L-malate was examined in the isolated MLF bacterium (MLB-S-6 strain) and the culture strains Leuc. mesenteroides IAM 1233,Lactobacillus casei IAM 1118,Lactobacillus plantarum IAM 1216,Lactobacillus arabinosus IAM 1041,and Streptococcus lactis RIB 806. All of the tested strains preadapted to malic acid converted L-malate to L-lactate within the range of pH 3.2-7.0. the optimal pH was 4-5 and the reaction was not inhibited by semicarbazide. On the other hand, D-lactate and acetate were produced from L-malate at higher pH, though generally much less D-lactate was formed than L-lactate. Leuc. mesenteroides also converted pyruvate to D-lactate and acetate whthin the range of pH 5-7. The optimal pH was 6.0 and the reaction was completely inhibited by semicarbazide (2,000ppm). A cell-free extract of Leuc. mesenteroides strain (MLB-S-6,IAM 1233) converted L-malate to L-lactate in the presence of NAD, Mn^〓 and semicarbazide. The specific activities were higher than those of the other tested strains. These results suggest than L-lactate in the wine was formed mainly from L-malate by malo-lactic enzyme, which directly converted L-malate to L-lactate. D-or L-lactate migth also in part be formed via pyruvate by the consecutive action of malic enzyme and D- or L-lactate dehydrogenase, especially in wine of high pH or when undesirable lactic aicd bacteria grow in the wine.