Sucrose and Other Disaccharides

Avigad, Gad

doi:10.1007/978-3-642-68275-9_7

Cited by 152 publications

(125 citation statements)

References 917 publications

Supporting

Mentioning

117

Contrasting

Order By: Relevance

“…1). Such apparently uncoordinated fluctuations of the fructose concentration and the 1 -FEH activity in dormant tubers might be due to two processes: First, in dormant tubers free fructose may be recycled for the synthesis and accumulation of sucrose (Avigad, 1982;Frehner, Keller & Wiemken, 1984). Second, plant FEH is inhibited by sucrose (Edelman & Jefford, 1964;Claessens et al, 1990;Simpson et al, 1991;Bonnett & Simpson, 1995) (Fig.…”

Section: -Feh Activity and Degradation Of Fructan In Vivomentioning

confidence: 99%

Seasonal variation of fructan‐β‐fructosidase (FEH) activity and characterization of a β‐(2‐1)‐linkage specific FEH from tubers of Jerusalem artichoke (Helianthus tuberosus)

1997

View full text Add to dashboard Cite

SUMMARYThe fructan-y?-fructosidase activity (1-FEH; EC 3.2.1.80) that degrades inulin in tubers oi Helianthus tuberosus L. appears to be developmentally regulated; it was low in growing tubers but increased during dormancy and sprouting. In spite of relatively high 1-FEH activity in vitro, fructose concentration was very low in developing and dormant tubers and increased markedly only during sprouting. A fructan-/S-fructosidase from such sprouting tubers was purified 41-fold to a single protein band on one-dimensional sodium dodecylsulphate-polyacrylamide gels. The purification procedure included ammonium sulphate precipitation, lectin-affinity chromatography on concanavalin A, anion-exchange and cation-exchange chromatography. The enzyme had an apparent molecular mass of 75000 measured by size-exclusion chromatography, and 79000 measured by one-dimensional sodium dodecylsulphate-polyacrylamide gel electrophoresis. It exhibited a high substrate specificity, hydrolysing terminal /?-(2-l)-fructosyl-fructose-linkages in linear and branched fructan oligomers; y^-(2-6)-linkages were hardly hydrolysed. Hydrolysis of inulin oligomers followed normal saturation kinetics: K^ values for 1,1-kestotetraose and 1,1,1-kestopentaose were 8-3 mM and 12 mM, respectively. Fructosyl residues were hydrolysed from inulin oligomers by a multi-chain mechanism. The fructan-y?-fructosidase showed optimal enzyme activity at pH 5-2, and it retained its full activity after pre-incubation for 1 h at up to 40 °C. The release of fructose from 5 mM 1,1-kestotetraose was reduced by 25 % when 1-FEH was assayed in the presence of 10 mM sucrose. It is proposed that the inhibition of 1-FEH activity by sucrose is a mechanism for controlling fructan degradation in planta.

show abstract

Section: -Feh Activity and Degradation Of Fructan In Vivomentioning

confidence: 99%

Seasonal variation of fructan‐β‐fructosidase (FEH) activity and characterization of a β‐(2‐1)‐linkage specific FEH from tubers of Jerusalem artichoke (Helianthus tuberosus)

1997

View full text Add to dashboard Cite

show abstract

“…Sucrose is the major transport form of carbon in the majority of plants. Correspondingly, SPS is present at high activities in source tissues such as mature leaves and germinating seeds (Avigad 1982). SPS is also present in sink tissues, where it may have additional roles.…”

Section: Introductionmentioning

confidence: 99%

Potato plants contain multiple forms of sucrose phosphate synthase, which differ in their tissue distributions, their levels during development, and their responses to low temperature

Reimholz¹,

Geiger²,

Haake³

et al. 1997

Plant Cell & Environment

View full text Add to dashboard Cite

Antibodies raised against a peptide fragment (residues 60-456) of potato sucrose phosphate synthase (SPS) were used to investigate whether potato plants contain multiple forms of SPS. When a partially purified preparation of SPS from cold-stored potato tubers was separated on 5 % polyacrylamide gel electrophoresis (PAGE), four immunopositive bands were found with estimated molecular weights of 125, 127, 135 and 145 kDa. These bands were also found in rapidly prepared extracts and were termed SPS-la, SPS-lb, SPS-2 and SPS-3, respectively. Direct evidence that SPS-la and SPS-lb represent active SPS was provided by the finding that both are greatly reduced in plants expressing an antisense sequence derived from the potato leaf SPS gene. SPS-2 was not decreased in the antisense plants, indicating that it has a significantly different sequence. Evidence that SPS-2 represents active SPS was obtained by showing that the amount of SPS-la and SPS-lb protein remaining in the leaves and tubers of antisense potato plants was too low to account for the remaining SPS activity. The four immunopositive SPS forms had different tissue distributions. SPS-la was the major form in all tissues except petals, sepals and stamens. SPS-lb and SPS-2 were absent in very young growing tissues hut were present as minor forms in source leaves and sprouting tubers. The SPS-lh level was especially high in petals and sepals, and the SPS-

show abstract

“…These include fructose, inulobiose or levanbiose, di-D-fructose dianhydrides, oligofructans and fructose-only oligomers (Iizuka & Yamamoto, 1979;Vandamme & Derycke, 1983;Ettalibi & Baratti, 1987). These numerous endproducts are presumed to be a result of the activities of different enzymes (Avigad, 1982). Uchiyama (1993) classified microbial enzymes according to their affinity for the t^^pe of linkage of fructan and for the site of cleavage inside the fructose chain.…”

Section: Introductionmentioning

confidence: 99%

Purification and substrate specificity of an extracellular fructanhydrolase from Lactobacillus paracasei ssp. paracasei P 4134

MÜLLER

SEYFARTH

1997

New Phytologist

View full text Add to dashboard Cite

SUMMARYA novel extracellular fructanhydrolase was isolated from the culture filtrate of Lactobacillus paracasei ssp. paracasei P4134 grown on a mineral medium supplemented with fructan extracted from Timothy {Phleum pratense L.) as the only carbon source. The enzyme was purified by a combination of ammonium sulphate precipitation, affinity chromatography, preparative isoelectric focusing and anion-exchange chromatography. As a result of these procedures, the specific enzyme activity increased 93-fold, with a final yield of 28-4%. The substrate-specific activities against different fructan types were determined by incubating the enzyme fractions with fructan extracted from Timothy (predominantly /5-2,6 fructosyl-fructose linkages), inulin from Dahlia tubers (mostly /?-2,l fructosyl-fructose linkages) and sucrose. The purified enzyme catalysed the hydrolysis of /?-2,6-linked fructan more rapidly than the /?-2,l linkages of inulin. Additionally, the enzyme showed low ability to hydrolyse sucrose. Fructose was the main product of the degradation of Timothy fructan and inulin, indicating a high exohydrolytic activity of the enzyme. It is proposed that the fructan-degrading enzyme from L. paracasei ssp. paracasei P 4134 is a /?-D-fructan-fructohydrolase (EC 3.2.1.80). The enzyme preparation showed a single protein band in sodium dodecyl sulphate-polyacrylamide gel electrophoresis with a mobility corresponding to molecular weight of c. 42 kDa. It was concluded that only one molecular weight of fructan-degrading enzyme exists in L. paracasei ssp. paracasei P 4134.

show abstract

Sucrose and Other Disaccharides

Cited by 152 publications

References 917 publications

Seasonal variation of fructan‐β‐fructosidase (FEH) activity and characterization of a β‐(2‐1)‐linkage specific FEH from tubers of Jerusalem artichoke (Helianthus tuberosus)

Seasonal variation of fructan‐β‐fructosidase (FEH) activity and characterization of a β‐(2‐1)‐linkage specific FEH from tubers of Jerusalem artichoke (Helianthus tuberosus)

Potato plants contain multiple forms of sucrose phosphate synthase, which differ in their tissue distributions, their levels during development, and their responses to low temperature

Purification and substrate specificity of an extracellular fructanhydrolase from Lactobacillus paracasei ssp. paracasei P 4134

Contact Info

Product

Resources

About