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2 0 0 0 人は時代といかに向き合うか

著者: 三谷太一郎著
出版者: 東京大学出版会
巻号頁・発行日: 2014

https://ci.nii.ac.jp/ncid/BB15865947

2 0 0 0 声優ラジオ"愛"史 : 声優とラジオの50年

著者: 村上謙三久著
出版者: 辰巳出版
巻号頁・発行日: 2019

https://ci.nii.ac.jp/ncid/BB29476284

2 0 0 0 日本政治思想史

著者: 丸山眞男著
出版者: 東京大学出版会
巻号頁・発行日: 1998

https://ci.nii.ac.jp/ncid/BA35646632

2 0 0 0 チェコ語

著者: 保川亜矢子著
出版者: 白水社
巻号頁・発行日: 2007

https://ci.nii.ac.jp/ncid/BA83616461

2 0 0 0 本の雑誌の坪内祐三

著者: 坪内祐三著
出版者: 本の雑誌社
巻号頁・発行日: 2020

https://ci.nii.ac.jp/ncid/BB31503255

2 0 0 0 OA 糸状菌グルコアミラーゼの構造と機能に関する研究

著者: 安部淳一
出版者: The Japanese Society of Applied Glycoscience
雑誌: 澱粉科学 (ISSN:00215406)
巻号頁・発行日: vol.36, no.1, pp.51-57, 1989-03-31 (Released:2010-06-28)
参考文献数: 20

(1) One form and three forms (GI, GII, and GIII) of glucoamylases were purified from crude commercial preparation of Aspergillus niger and Rhizopus delemar, respectively, to be homogenous on disc- and SDS-gel electrophoresis and free from a-amylase and phosphatase. Neither purified glucoamylase from A. niger nor R. delemar could completely hydrolyze various kinds of starches because of the presence of phosphate esters attached to C-3 or C-6 of glucosyl residue, and left a limit-dextrin of large-molecular weight. The concomitant actions of a-amylase and phosphatase with the glucoamylases were found to be necessary for complete hydrolysis of these starches. (2) R. delemar GIII was suggested to have a specific affinity site, "starch-binding site, " for high-molecular-weight substrates from the results of kinetic study and modification with chymotrypsin. GI and GII were suggested to be derived from GIII by the post-secretional modification. (3) Aspergillus sp. K-27 produced the enzyme (s) which degraded well the raw starches. Glucoamylase and a-amylase were separated and purified from the culture filtrate of the fungus. The former seemed to have the "starch-binding site, " based on the results of partial proteolysis and kinetic studies. The latter showed low activity on raw starches but synergistically enhanced the degradation of starch granules with glucoamylase. The removal of the starch-binding site from glucoamylase reduced the ability of raw-starch degradation and abolished the synergistic effect with a-amylase. These results suggested that the starch-binding site plays an importantrole in raw-starch hydrolysis.