Screening Test for Xylanolytic Activities of Commercially Available Enzymes and Release of Arabinose from Arabinoglucuronoxylan by the Enzymes.
-
- Park Nyun Ho
- Institute of Applied Biochemistry, University of Tsukuba
-
- Yoshida Shigeki
- Institute of Applied Biochemistry, University of Tsukuba
-
- Kawabata Yasuyuki
- Akita Research Institute of Food and Brewing
-
- Sun Hyeon Jin
- Institute of Applied Biochemistry, University of Tsukuba
-
- Kusakabe Isao
- Institute of Applied Biochemistry, University of Tsukuba
Bibliographic Information
- Other Title
-
- 市販酵素製剤のキシラン分解酵素系の選別試験と同酵素剤によるアラビノキシランからアラビノースの遊離
Search this article
Abstract
Twenty-three kinds of commercially available enzymes were subjected to the screening test for xylanolytic activities, namely, endo-β-xylanase, β-xylosidase, α-arabinofuranosidase and α-glucuronidase.The majority of the enzymes contained some of the activities. The above enzymes were also submitted to the hydrolyzable test on the arabinoglucuronoxylan of corn hull. Among them, Cellulase C-0901 (Sigma Chemicals) originating from Penicillium funiculosum, although lacking in a-glucuronidase, degraded the xylan very well, and released 80.5% of arabinose and 60.8% of xylose based on the component sugars of the xylan. On the other hand, Cellulase 'Onozuka' R-10 (Yakult Co.) originating from Trichoderma viride, although containing all of the xylanolytic activities, decomposed hardly any of the arabinoglucuronoxylan. According to these results, commer cially available enzymes contained high and various xylanolytic activities. However, the intensities of enzyme activity and hydrolyzable ability differed remarkably in the degradation of arabinogluc uronoxylan. In addition, Cellulase C-0901 was most suitable among them for the enzymatic hydrolysis of the xylan.
Journal
-
- Journal of Applied Glycoscience
-
Journal of Applied Glycoscience 48 (3), 253-262, 2001
The Japanese Society of Applied Glycoscience
- Tweet
Details 詳細情報について
-
- CRID
- 1390001206293877888
-
- NII Article ID
- 10008252836
-
- NII Book ID
- AN10453916
-
- ISSN
- 13403494
- 18807291
- 13447882
-
- NDL BIB ID
- 5831490
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
-
- Abstract License Flag
- Disallowed