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Please use this identifier to cite or link to this item: http://hdl.handle.net/11178/4601

Title: Bacillus subtilis 3108株の産生する生澱粉分解性α-アミラーゼの特性(物質生命化学科)
Other Titles: Properties of raw starch digesting α-amylase from Bacillus subtilis IFO 3108(DEPARTMENT OF APPLIED CHEMISTRY AND BIOCHENISTRY)
Authors: 山口, 哲平
木村, 弘幸
川野, 麻里子
原, 三貴子
満生, 慎二
境, 正志
Yamaguchi, Teppei
Kimura, Hiroyuki
Kawano, Mariko
Hara, Mikiko
Mitsuiki, Shinji
Sakai, Masashi
ヤマグチ, テッペイ
キムラ, ヒロユキ
カワノ, マリコ
ハラ, ミキコ
ミツイキ, シンジ
サカイ, マサシ
九州産業大学工学研究科 / 九州産業大学工学部工業化学科 / 九州産業大学工学部工業化学科 / 九州産業大学工学部工業化学科 / 九州産業大学工学部物質生命化学科 / 九州産業大学工学部物質生命化学科
Keywords: Raw starch
Bacillus sp.
Starch affinity domain
Issue Date: 20-Dec-2005
Publisher: 九州産業大学工学部
Abstract: α-Amylases from Bacillus sp. strains digesting raw starch were observed to adsorb to raw starch and α-cyclodextrin (CD) Sepharose. Raw starch digesting and saccharyfying α-amylases was purified from Bacillus subtilis IFO 3108 (RSA-1, MM 67 kDa). BSA1 was able to adsorb to α-CD Sepharose and to digest raw starch. The other amylase from the strain was unable to adsorb to α-CD Sepharose CL-6B and failed to digest raw starch. The digest of raw corn starch was specifically inhibited by α-CD for BSA1 (Ki, 0.44mM). The adsorption ability of BSA1 to α-CD Sepharose had not lost upon protease treatment. Results indicate that although raw starch affinity domain (SAD) involved is present in BSA1, the structure and mode of binding of SAD are different from other amylases.
URI: http://hdl.handle.net/11178/4601
Appears in Collections:第42号

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