Purification and Characterization of an α-L-Rhamnosidase from Pichia angusta X349
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概要
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An intracellular α-L-rhamnosidase from Pichia angusta X349 was purified to homogeneity through four chromatographic steps. The α-L-rhamnosidase appeared to be a monomeric protein with a molecular mass of 90 kDa. The enzyme had an isoelectric point at 4.9,and was optimally active at pH 6.0 and at around 40℃. The Ki for L-rhamnose inhibition was 25 mM. The enzyme was inhibited by Cu^<2+>, Hg^<2+>, and p-chloromercuribenzoate. The α-L-rhamnosidase was highly specific for α-L-rhamnopyranoside and liberated rhamnose from naringin, rutin, hesperidin, and 3-quercitrin. The α-L-rhamnosidase was active at the ethanol concentrations of wine. It efficiently released monoterpenols, such as linalool and geraniol, from an aroma precursor extracted from Muscat grape juice.
- 社団法人日本農芸化学会の論文
- 2000-10-23
著者
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YANAI Takaaki
Mercian Corporation
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Yanai T
Mercian Corp. Fujisawa Jpn
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SATO Michikatsu
Mercian Corporation, Wine & Spirits Research Institute
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Sato Michikatsu
Mercian Corporation Wine & Spirits Research Institute
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