Purification and characterisation of 6G-fructosyltransferase from the roots of asparagus (Asparagus officinalis L.)
書誌事項
- 公開日
- 1981-10
- 権利情報
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- https://www.elsevier.com/tdm/userlicense/1.0/
- DOI
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- 10.1016/s0008-6215(00)81878-9
- 公開者
- Elsevier BV
この論文をさがす
説明
Abstract A fructosyltransferase that transfers a terminal d -fructosyl group from a (2→1)-β-linked fructosaccharide to HO-1 of another d -fructosyl group has been purified from an extract of asparagus roots by successive chromatography with DEAE-cellulose, octyl-Sepharose, Sephadex G-200, and raffinose-coupled Sepharose 6B. The disc-electrophoretically homogeneous enzyme was free from β- d -fructofuranosidase, sucrose:sucrose 1-fructosyltransferase, and 6G-frutosyltransferase activity, and catalysed the d -fructosyl transfer from 1-kestose more rapidly to saccharides of the neokestose series [1F(1-β- d -fructofuranosyl)m-6G(1-β- d -fructofuranosyl)nsucrose] than to those of the 1-kestose series [1F(1-β- d -fructofuranosyl)nsucrose]. The enzyme was tentatively termed 1F-fructosyltransferase. The general properties of the enzyme were as follows: mol. wt., ~64,000; optimum pH, ~5.0; stable at pH 5.0–5.5 at 45° for 20 min; stable at 30–45° for 10 min; inhibited by Hg2+, p-chloromercuribenzoate, and Ag+.
収録刊行物
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- Carbohydrate Research
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Carbohydrate Research 96 (2), 281-292, 1981-10
Elsevier BV