Studies on yeast invertase. Soluble and insoluble invertase (saccharase) of baker's yeast

Myrbäck, Karl

doi:10.1016/0003-9861(57)90481-2

Cited by 27 publications

(5 citation statements)

References 9 publications

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“…Invertases (β- d -fructofuranosidases, EC 3.2.1.26), widely distributed among plants and microorganisms, catalyse the hydrolysis of sucrose to equimolar amounts of d- fructose and d- glucose [1]. At saturated (high) sucrose concentrations, many β-fructofuranosidases – especially those of fungal origin – display varying degrees of fructosyltransferase activity by cleaving the β-(2 → 1) linkage, releasing glucose, and transferring the fructose moiety onto an acceptor molecule other than water.…”

Section: Introductionmentioning

confidence: 99%

Identification of the gene for β-fructofuranosidase from Ceratocystis moniliformis CMW 10134 and characterization of the enzyme expressed in Saccharomyces cerevisiae

et al. 2013

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Backgroundβ-Fructofuranosidases (or invertases) catalyse the commercially-important biotransformation of sucrose into short-chain fructooligosaccharides with wide-scale application as a prebiotic in the functional foods and pharmaceutical industries.ResultsWe identified a β-fructofuranosidase gene (CmINV) from a Ceratocystis moniliformis genome sequence using protein homology and phylogenetic analysis. The predicted 615 amino acid protein, CmINV, grouped with an existing clade within the glycoside hydrolase (GH) family 32 and showed typical conserved motifs of this enzyme family. Heterologous expression of the CmINV gene in Saccharomyces cerevisiae BY4742∆suc2 provided further evidence that CmINV indeed functions as a β-fructofuranosidase. Firstly, expression of the CmINV gene complemented the inability of the ∆suc2 deletion mutant strain of S. cerevisiae to grow on sucrose as sole carbohydrate source. Secondly, the recombinant protein was capable of producing short-chain fructooligosaccharides (scFOS) when incubated in the presence of 10% sucrose. Purified deglycosylated CmINV protein showed a molecular weight of ca. 66 kDa and a Km and Vmax on sucrose of 7.50 mM and 986 μmol/min/mg protein, respectively. Its optimal pH and temperature conditions were determined to be 6.0 and 62.5°C, respectively. The addition of 50 mM LiCl led to a 186% increase in CmINV activity. Another striking feature was the relatively high volumetric production of this protein in S. cerevisiae as one mL of supernatant was calculated to contain 197 ± 6 International Units of enzyme.ConclusionThe properties of the CmINV enzyme make it an attractive alternative to other invertases being used in industry.

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Section: Introductionmentioning

confidence: 99%

Identification of the gene for β-fructofuranosidase from Ceratocystis moniliformis CMW 10134 and characterization of the enzyme expressed in Saccharomyces cerevisiae

et al. 2013

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“…Apart from the irradiation studies already mentioned and the effect of pH and inhibitors on the invertase of living cells (Myrback & Willstaedt, 1955;Myrback, 1957) there are other grounds for associating invertase with the cell wall. Many attempts to purify the enzyme have led to the realization that it is closely associated with polysaccharide (cf.…”

Section: Discussionmentioning

confidence: 99%

“…Recently Myrback (1957) drew attention to the effect of ethyl acetate on baker's yeast. Cells treated overnight and washed thoroughly with water on the centrifuge lose much of their contents but retain the greater part of their invertase, even when stored for several months.…”

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confidence: 99%

Some observations on the form and location of invertase in the yeast cell

Burger¹,

Bacon²,

Bacon³

1961

Biochemical Journal

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“…Major attention was directed to industrial strains of Saccharomyces, although Hansenula and related nonascosporogenous yeasts have been important in this field. In 1957, MyrbAck (18) reported that in the baker's yeast he studied, the enzyme in its native state is insoluble and tightly bound to other cell constituents. Burger, Bacon, and Bacon (4) believed that the invertase in another strain of baker's yeast was soluble; after they crushed the live yeast a large proportion of its invertase was liberated in a water-soluble form.…”

Section: E Invertasementioning

confidence: 99%