2021
DOI: 10.1016/j.procbio.2021.08.016
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Transglycosylation properties of a Kluyveromyces lactis enzyme preparation: Production of tyrosol β-fructoside using free and immobilized enzyme

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Cited by 7 publications
(3 citation statements)
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“…Moreover, many microeukaryotic genera were positively related to the development of terpenoids and flavonoids in icewine. It is due to these compounds commonly present in glycosidic bound forms, while the epiphytic microeukaryotes of grapes can generate a series of glycoside hydrolases (GHs) and glycosyl transferases (GTs), which efficiently break glycosidic bonds and release the aglycones [2,31]. For instance, monoterpenyl disaccharide glycosides originated from plants and microbes, such as α-arabinofuranosidase, β-glycosidase, and β-galactosidase, hydrolyze glycosidic bound terpenes into free forms [32].…”
Section: Discussionmentioning
confidence: 99%
“…Moreover, many microeukaryotic genera were positively related to the development of terpenoids and flavonoids in icewine. It is due to these compounds commonly present in glycosidic bound forms, while the epiphytic microeukaryotes of grapes can generate a series of glycoside hydrolases (GHs) and glycosyl transferases (GTs), which efficiently break glycosidic bonds and release the aglycones [2,31]. For instance, monoterpenyl disaccharide glycosides originated from plants and microbes, such as α-arabinofuranosidase, β-glycosidase, and β-galactosidase, hydrolyze glycosidic bound terpenes into free forms [32].…”
Section: Discussionmentioning
confidence: 99%
“…To overcome the many drawbacks of free lipase, enzyme immobilization techniques have been investigated. In comparison to the free enzyme, the immobilized enzyme has several advantages, such as easier separation and recycling, higher activity, more stable enzymes, more resistance to various environmental changes, non-toxicity and biocompatibility, or coupling with enzyme purification, making it suitable for more complex reaction environments and a variety of reactor configurations [ 3 , 10 , 11 , 12 ]. However, some lipases react with hydrophobic matrixes or other lipase molecules during the immobilization process, resulting in lipase inactivation.…”
Section: Introductionmentioning
confidence: 99%
“…The latter ones facilitate the biocatalytic process by excluding the tedious cultivation and purification step to obtain FTases with sufficient transfructosylation activity [14,15]. Many commercial enzyme preparations (pectinases, polygalacturonases, and glucanases) also have the potential to produce FOS because of their FTase side activity [15][16][17].…”
Section: Introductionmentioning
confidence: 99%