Enzymatic Conversion of Anthraquinone Pigment Originated from Madder and Product Extraction in Batch Reaction.
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- Masawaki Teruyuki
- Dept. of Chem. Eng., Osaka Univ.
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- Tobo Kazuhisa
- Dept. of Chem. Eng., Osaka Univ.
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- Taya Masahito
- Dept. of Chem. Eng., Osaka Univ.
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- Tone Setsuji
- Dept. of Chem. Eng., Osaka Univ.
Bibliographic Information
- Other Title
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- 回分反応におけるセイヨウアカネ由来のアントラキノン色素の酵素変換と生成物抽出
- カイブン ハンノウ ニ オケル セイヨウアカネ ユライ ノ アントラキノン シ
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Abstract
Enzymatic hydrolyses of anthraquinone glycosides (Alizarin-2-ο-primeveroside (Al-P) and Lucidin-3-ο-primeveroside (Lu-P)) from madder plant were examined for the formation and separation of the useful pigment, alizarin. Among enzymes tested in this study, almond-derived β-glucosidase showed the highest hydrolytic activity and reaction selectivity for Al-P. Hydrolyses of anthraquinone glycosides were carried out in a batch operation by using the β-glucosidase immobilized by covalent linkage to fine powders of TiO2, and it was found that the formed alizarin exerted an inhibitory effect on the enzyme reaction.<BR>Separation and recovery of alizarin in a hexane phase were performed by combining solvent extraction with enzyme reaction, reducing the inhibitory effect on the reaction caused by alizarin. Taking into account the partition equilibrium between the aqueous and hexane phases, time profiles of the formation and extraction processes of alizarin were successfully expressed in a batch operation by a Michaelis-Menten equation considering the product inhibition.
Journal
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- KAGAKU KOGAKU RONBUNSHU
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KAGAKU KOGAKU RONBUNSHU 22 (4), 891-897, 1996
The Society of Chemical Engineers, Japan
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Keywords
Details 詳細情報について
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- CRID
- 1390001204510332288
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- NII Article ID
- 10002669264
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- NII Book ID
- AN00037234
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- ISSN
- 13499203
- 0386216X
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- NDL BIB ID
- 3995447
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed