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Studies on Maltotriose- and Maltose-forming Amylases from Streptomyces
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- WAKO Katsuo
- Nikken Chemical Co., Ltd.
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- TAKAHASHI Chikanori
- Nikken Chemical Co., Ltd.
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- HASHIMOTO Seiji
- Nikken Chemical Co., Ltd.
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- KANAEDA Jun
- Nikken Chemical Co., Ltd.
Bibliographic Information
- Other Title
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- マルトトリオースおよびマルトースを生成する2種放線菌アミラーゼ
- マルトトリオース オヨビ マルトース オ セイセイスル 2シュ ホウセンキン
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Description
Two amylases produced by Streptomyces were purified, and some properties were studied. The one, named NA-468 amylase, was produced by a strain of Streptomyces griseus and formed about 55% of maltotriose from starch. NA-468 amylase was purified to almost 100-fold of the culture broth, and showed its maximal activity at 45°C and pH 5.6-6.0. Amylose was hydrolyzed to almost 100%, but waxy starch Q-limit dextrin was not acted. It was found that NA-468 amylase cleaved the third glucosidic bond from the end of the maltooligosaccharide. The other one, named NA-273 amylase, was produced by a strain of Streptomyces praecox, and formed more than 80% of maltose from starch. NA-273 amylase was purified to about 170-fold, and showed its maximal activity at 47°C and pH 6.0. Acting on amylose, soluble starch and waxy starch β-limit dextrin, the amylase produced a large amount of α-maltose. The amylase also hydrolyzed maltotriose to form maltose without the formation of glucose. The action mechanism of it was considered that glucose formed by hydrolysis was transferred to the non-reducing end of other maltotriose, and that maltotetraose formed was again hydrolyzed to maltose.
Journal
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- Journal of the Japanese Society of Starch Science
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Journal of the Japanese Society of Starch Science 25 (2), 155-161, 1978
The Japanese Society of Applied Glycoscience
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Details 詳細情報について
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- CRID
- 1390282681269669632
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- NII Article ID
- 130003866457
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- NII Book ID
- AN00154431
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- ISSN
- 1884488X
- 00215406
- http://id.crossref.org/issn/0015749X
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- NDL BIB ID
- 1922317
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL Search
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed