http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Jia-Yan Liu,Gao-Wei Zheng,Tadayuki Imanaka,Jian-He Xu 한국생물공학회 2014 Biotechnology and Bioprocess Engineering Vol.19 No.3
Optically pure 1-(3’,4’-methylenedioxyphenyl)ethanol is a key chiral intermediate for the synthesis ofSteganacin and Salmeterol. A para-nitrobenzyl esterasecloned from Bacillus amyloliquefaciens (BAE) was employedto hydrolyze 1-(3’,4’-methylenedioxyphenyl) ethyl ester forthe production of (R)-1-(3’,4’-methylenedioxyphenyl)ethanol. Initially, a moderate enantioselectivity (E = 35) only wasobtained at 30°C. Some reaction conditions such asreaction temperature and additive approach were investigatedin order to improve the enantioselectivity of the BAEcatalyzedreaction.. As a result, the enantioselectivity wasimproved significantly to 140 under addition of Tween-80and a decreasing reaction temperature to 0°C. The resultwas confirmed in a decagram-scale preparative bioresolutionalso. The optimized enzymatic hydrolysis conditions providea more effective process for the (R)-1-(3’,4’-methylenedioxyphenyl)ethanol bioproduction.
Atomic Force Microscopic Study of Chitinase Binding onto Chitin and Cellulose Surfaces
Kikkawa, Yoshihiro,Fukuda, Masato,Kimura, Tomoya,Kashiwada, Ayumi,Matsuda, Kiyomi,Kanesato, Masatoshi,Wada, Masahisa,Imanaka, Tadayuki,Tanaka, Takeshi American Chemical Society 2014 Biomacromolecules Vol.15 No.3
<P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bomaf6/2014/bomaf6.2014.15.issue-3/bm500046f/production/images/medium/bm-2014-00046f_0004.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/bm500046f'>ACS Electronic Supporting Info</A></P>
FUJIWARA, SHINSUKE,KAKIHARA, HIROFUMI,KIM, BYUNG WOO,LEJEUNE, ANDRE,KANEMOTO, MITSUHIDE,SAKAGUCHI, KENJI,IMANAKA, TADAYUKI 동의대학교 기초과학연구소 1993 基礎科學硏究論文集 Vol.3 No.1
Cyclodextrin glucanotransferase (CGTase; EC 2.4.1.19) is produced mainly by Bacillus strains. CGTase from Bacillus macerans IFO3490 produces α-cyclodextrin as the major hydrolysis product from starch, where as thermostable CGTase from Bacillus stearothermophilus NO2 produces α- and β- cyclodextrins. To analyze the cyclization characteristics of CGTase, we cloned different types of CGTase genes and constructed chimeric-genes. CGTase genes from these two strains were cloned in Bacillus subtilis NA-1 by using pTB523 as a vector plasmid, and their nucleotide sequences were determined. Three CGTase genes (cgt-1, cgt-5, and cgt-232) were isolated from B. stearothermophilus NO2. Nucleotide sequence analysis revealed that the three CGTase genes have different nucleotide sequences encoding the same amino acid sequence. Base substitutions were found at the third letter of five codons among the three genes. Each open reading frame was composed of 2,133 bases, encoding 711 amino acids containing 31 amino acids as a signal sequence. The molecular weight of the mature enzyme was estimated to be 75,374. The CGTase gene (cgtM) of B. macerans IFO3490 was composed of 2,142 bases, encoding 714 amino acids containing 27 residues as a signal sequence. The molecular weight of the mature enzyme was estimated to be 74,008. The sequence determined in this work was quite different from that reported previously by other worker. From data on the three-dimensional structure of a CGTase, seven kinds of chimeric CGTase genes were constructed by using cgy-1 from B. stearothermophilus NO2 and cgtM from B. macerans IFO3490. We examined the characteristics of these chimeric enzymes on cyclodextrin production and thermostability. It was found that the cyclization reaction was conferred by the NH₂-terminal region of CGTase and that the thermostability of some chimeric enzymes was lower than that of the parental CGTases.
Jun Tan,Ju Chu,Wenjuan Shi,Cheng Lin,Yuanxin Guo,Ying-ping Zhuang,Siliang Zhang,Tadayuki Imanaka 한국식품과학회 2012 Food Science and Biotechnology Vol.21 No.6
Most of the fermentation experiment designs were limited by the low-throughput of shake flask, especially for the medium optimization. A simple high-throughput screening system was developed for the determination of pigment in Monascus purpureus fermentation samples. This downscaled system was designed to optimize medium composition combined with statistical methods. The total 29 experiments designed by the Box–Behnken were used to study the 4 most important operating variables on pigment production. The analysis revealed that the optimum concentrations of glucose, peptone, NaNO3, and KH2PO4were 51.42, 4.91, 1.00, and 1.00 g/L, respectively. A production of 69.5 U/mL was achieved in agreement with the prediction (68.9 U/mL) fermented in 24-deep-well microtiterplates. Furthermore, the fermentation medium optimized in the high-throughput system was verified in shake flasks, and the pigment production could be enhanced from 206.5 U/mL in un-optimized medium to 265.8 U/mL,giving nearly 1.30-fold increase in production.