HOME    Nuar Information    mypage        Japanese    Feedback

新潟大学学術リポジトリ Nuar >
070 農学部 = Faculty of Agriculture >
10 学術雑誌論文 = Journal Article >
10 査読済論文 = Postprint >

 

Files in This Item:

File Description SizeFormat
ZM_5(1)_18-23.pdf818KbAdobe PDF
Title :Purification and Characterization of Phytase from Bran of Triticum aestivum L. cv. Nourin #61
Authors :Nakano, Tadao
Joh, Toshio
Tokumoto, Emi
Hayakawa, Toshiro
Publisher :日本食品科学工学会
Issue Date :Feb-1999
Journal Title :Food Science and Technology research
Volume :5
Issue :1
Start Page :18
End Page :23
ISSN :1344-6606
Abstract :Two phytase isozymes (PHY1 and PHY2) were purified homogeneously from bran of Triticum aestivum L. cv. Nourin #61 by (NH4)2SO4 fractionation, methanol fractionation, Sephacryl S-200 HR gel filtration chromatography, DEAE-TOYOPEARL chromatography, CM-TOYOPEARL chromatography and second Sephacryl S-200 HR gel filtration chromatography. Molecular weights of the two enzymes were 71,000 and 66,000 by gel filtration, and 68,000 and 66,000 by SDS-PAGE, respectively. Optimum pH and temperatures were 6.0 and 45℃ for PHY1, and 5.5 and 50℃ for PHY2. The activity of both phytases was stable at pHs between pH 4.0-7.0 and below 40℃. The Km values for myo-inositol hexakisphosphate (IHP) were 0.48 μM for PHY1 and 0.77 μM for PHY2. The Ki values for Pi were 2.69 mM for PHY1 and 6.59 mM for PHY2. Both phytases showed relatively high specificity for IHP.
Keywords :phytase
phytic acid
wheat bran
Nourin #61
purification
Type Local :学術雑誌論文
Language :eng
Format :application/pdf
URI :http://hdl.handle.net/10191/17598
fullTextURL :http://dspace.lib.niigata-u.ac.jp/dspace/bitstream/10191/17598/1/ZM_5(1)_18-23.pdf
Rights :社団法人日本食品科学工学会
Appears in Collections:10 査読済論文 = Postprint

Please use this identifier to cite or link to this item: http://hdl.handle.net/10191/17598