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   <subfield code="a">Isolation and Characterization of an Enzyme with β-Glucosidase and β-Fucosidase Activities from Dalbergia cochinchinensis Pierre</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Chantragan Srisomsap, Jisnuson Svasti, Rudee Surarit, Voraratt Champattanachai, Phannee Sawangareetrakul, Kanokporn Boonpuan, Pantipa Subhasitanont, Daranee Chokchaichamnankit]</subfield>
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   <subfield code="a">A glycosidase enzyme with both β-glucosidase and β-fucosidase activities has been purified from the seeds of Dalbergia cochinchinensis Pierre (Thai Rosewood) by ammonium sulfate fractionation, preparative isoelectric focusing, and Sephadex G-150 chro-matography. The enzyme has molecular weights of 330,000 in the native state and 66,000 in the denatured state. Hydrolysis of p-NP-β-D-glucoside and p-NP-β-D-fucoside showed pH optimum at pH 5.0 and was inhibited by Rcat-gluconolactone, HgCl2, and p-chloromercuri-benzoate. The Km and fecal values of the purified enzyme were 5.4 mM and 307 s1 for p-NP-β-D-glucoside and 0.54 mM and 151 s−1 for p-NP-β-D-fucoside, so that the latter had by far the higher kcat&amp;Km ratio. p-NP-β-D-galactoside, p-NP-β-D-xyloside, and p-NP-α-L-arabinoside were hydrolyzed more slowly. Hydrolysis of sophorose, laminaribiose, and gentiobiose were also rather slow, and hydrolysis of cellobiose was even slower. No hydrolysis of the cyanogenic glucosides linamarin or prunasin, but some hydrolysis of amygdalin and salicin was found. Further studies are required to identify the natural substrates of the enzyme. However, high yields, ease of purification, and storage stability of the enzyme make it a useful candidate for various applications, such as study of oligosaccharide synthesis by reversal of hydrolysis</subfield>
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   <subfield code="a">© by the Journal of Biochemistry</subfield>
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   <subfield code="a">Dalbergia spp</subfield>
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   <subfield code="a">β-glucosidase</subfield>
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   <subfield code="a">rosewood</subfield>
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   <subfield code="a">Srisomsap</subfield>
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   <subfield code="u">Laboratory of Biochemistry, Chulabhorn Research Institute Vibhavadee Rangsit Rd., Bangkok 10210, Thailand</subfield>
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   <subfield code="a">Svasti</subfield>
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   <subfield code="u">Laboratory of Biochemistry, Chulabhorn Research Institute Vibhavadee Rangsit Rd., Bangkok 10210, Thailand</subfield>
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   <subfield code="u">Laboratory of Biochemistry, Chulabhorn Research Institute Vibhavadee Rangsit Rd., Bangkok 10210, Thailand</subfield>
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   <subfield code="t">The Journal of Biochemistry</subfield>
   <subfield code="d">Oxford University Press</subfield>
   <subfield code="g">119/3(1996-03), 585-590</subfield>
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