1999
DOI: 10.1016/s0141-0229(98)00066-0
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Extraction and immobilization in one step of two β-glucosidases released from a yeast strain of Debaryomyces hansenii

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Cited by 29 publications
(16 citation statements)
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“…The enzyme did not hydrolyze the synthetic substrates with non-glucose sugar residues or containing the a glycosidic bond. In contrast, one b-glucosidase from D. hansenii reported by Riccio et al (1999) was capable of hydrolyzing different synthetic substrates with b and a configurations, indicating different features between b-glucosidases from these two strains. In relation to the natural substrates, the D. hansenii UFV-1 b-glucosidase was highly specific for the b-(1,4) linkage of glucose residues, since the enzyme was only able to hydrolyze cellobiose and cellulose.…”
Section: Resultsmentioning
confidence: 96%
“…The enzyme did not hydrolyze the synthetic substrates with non-glucose sugar residues or containing the a glycosidic bond. In contrast, one b-glucosidase from D. hansenii reported by Riccio et al (1999) was capable of hydrolyzing different synthetic substrates with b and a configurations, indicating different features between b-glucosidases from these two strains. In relation to the natural substrates, the D. hansenii UFV-1 b-glucosidase was highly specific for the b-(1,4) linkage of glucose residues, since the enzyme was only able to hydrolyze cellobiose and cellulose.…”
Section: Resultsmentioning
confidence: 96%
“…At this time, several studies have shown that in general yeasts involved in the fermentation processes have varying degrees of b-glucosidase activity. The highest degree of this activity has been found in non-Saccharomyces yeast strains, including B. bruxellensis, as opposed to S. cerevisiae (Rosi et al, 1994;McMahon et al, 1999;Riccio et al, 1999;Manzanares et al, 2000). This may outline a niche group of substrates that B. bruxellensis could be able to utilise in a more efficient manner than S. cerevisiae.…”
Section: Refined Cane Sugarmentioning
confidence: 98%
“…This enzyme was immobilized using a one-step procedure on hydroxyapatite. The immobilized enzyme exhibited a lower activity than the purified free enzyme, but was much more stable than the enzyme in cell-free supernatant [87]. Their studies have shown the ability of several wine yeasts to hydrolyse terpenoids, norisoprenoids and benzenoids glycosides; among wine yeasts H. uvarum was able to hydrolyze both glyco-conjugated forms of pyranic and furanic oxides of linalool [88].…”
Section: β-Glucosidasesmentioning
confidence: 99%