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pro vyhledávání: '"Hiroyuki Miyakubo"'
Autor:
Satoshi Nakamura, Yuko Osada, Hidenori Takahashi, Hiroyuki Miyakubo, Toshiaki Fukui, Tomoko Sakata, Rie Yatsunami, Rieko Wada
Publikováno v:
Journal of Applied Glycoscience. 53:131-136
Alkaliphilic Bacillus sp. strain 41M-1 secretes a xylanase (termed xylanase J) that has an alkaline pH optimum. Xylanase J is a multidomain enzyme and consists of two functional domains: a glycoside hydrolase family 11 catalytic domain and an additio
Autor:
Hiroyuki Miyakubo, Rieko Wada, Rie Yatsunami, Toshiaki Fukui, Tomoko Sakata, Satoshi Nakamura, Yuko Osada, Jun Takakura, Hidenori Takahashi
Publikováno v:
Nucleic acids symposium series (2004). (50)
Xylanase J (XynJ) of alkaliphilic Bacillus sp. strain 41M-1 is a multi-domain enzyme and consists of a glycoside hydrolase (GH) family 11 catalytic domain and an additional xylan-binding domain (XBD) belonging to carbohydrate-binding module (CBM) fam
Autor:
Hiroyuki Miyakubo, Akiko Sugio, Satoshi Nakamura, Kenji Wakabayashi, Takafumi Kubo, Ryuichiro Nakai
Publikováno v:
Scopus-Elsevier
Xylanase J from alkaliphilic Bacillus sp. strain 41M-1 has a family 11/G catalytic domain and a xylan-binding module (XBM). The XBM of xylanase J was displayed on the surface of filamentous bacteriophage. The XBM expressed on the phage surface retain