maltotriose/potato

The inhibitory effect of phosphorylated oligosaccharides, which were prepared from potato starch, on the formation of calcium phosphate in vitro were investigated. Phosphorylated oligosaccharides from potato were fractionated by ion-exchange chromatography into two fractions, PO-1 and PO-2. Fraction

Microbacterium aurum strain B8.A was isolated from the sludge of a potato starch-processing factory on the basis of its ability to use granular starch as carbon- and energy source. Extracellular enzymes hydrolyzing granular starch were detected in the growth medium of M. aurum B8.A, while the type

In the present study, hydrolysis of potato starch with marine cold-adapted α-amylase and pullulan production from the hydrolysates by a new strain of Auerobasidium pullulans isolated from sea mud were conducted. The hydrolysis conditions were optimized as follows: reaction time 2h, pH 6.5,

We have examined under a variety of conditions the ability of potato starch phosphorylase to cause exchange of the ester and phosphoryl oxygens of alpha-D-glucopyranose 1-phosphate (Glc-1-P). In the presence of phosphorylase and strach, under conditions where 40-50% of the glc-1-P is consumed in

The end products from starch hydrolysis by amylases have important applications in various industries. Here, two amylases derived from two Streptomyces species that hydrolyze soluble starch from potato produced maltotriose as the primary maltooligosaccharide product. The genes, annotated as putative

Sweet potato beta-amylase [EC 3.2.1.2, alpha 1,4-D-glucan maltohydrolase]-catalyzed hydrolyses of aryl beta-maltotriosides with substituents, NO2-, Cl-, and Br- at the o-, m-, and p-positions in the phenyl ring were studied at pH 4.8 and 25 degrees C. The hydrolyses of a few of the maltotriosides by

A maltotetraose- and maltotriose-producing amylase which is stable at alkaline pHs and high temperatures was detected in the culture filtrate of a strain of Chloroflexus aurantiacus J-10-F1, a thermophilic, green, photosynthetic bacterium. The enzyme was purified to homogeneity, as demonstrated by

A newly isolated bacterium, identified as Bacillus subtilis 65, was found to produce raw-starch-digesting alpha-amylase. The electrophoretically homogeneous preparation of enzyme (molecular weight, 68,000) digested and solubilized raw corn starch to glucose and maltose with small amounts of

Two glucanotransferases, disproportionating enzyme 1 (StDPE1) and disproportionating enzyme 2 (StDPE2), were repressed using RNA interference technology in potato, leading to plants repressed in either isoform individually, or both simultaneously. This is the first detailed report of their combined

Digestion of potato starch with His-modified alpha-cyclodextrin glycosyltransferase from Klebsiella pneumoniae M 5 al yielded branched tetra- to nona-saccharides, as revealed by debranching with pullulanase. Maltose and maltotriose stubs preponderated together with small proportions of D-glucose

The presence of carbohydrates and organic acids was monitored in the oral cavity over a 3-hour period following the ingestion of six foods containing cooked starch (popcorn, potato chips, corn flakes, bread stick, hard pretzel and wheat cracker) and compared to a food containing sugar

Oral carbohydrate clearance and acid production were monitored over a two hour time period following the ingestion of six foods (chocolate bar, potato chip, oreo cookie, sugar cube, raisin and jelly bean). Each food was evaluated intra-orally in eight volunteers. Oral fluid samples were obtained

Little information is yet available on the alpha-amylases of cyanobacteria. Here, the presence of an alpha-amylase in the cyanobacterium Nostoc sp. PCC 7119 is first demonstrated. A gene (amy1) encoding a cytoplasmic alpha-amylase (Amy1) protein has been identified, cloned, and overexpressed in

This paper describes thermostable phosphorylase-catalyzed α-glucuronylation of maltooligosaccharides for the direct synthesis of anionic oligosaccharides having a glucuronic acid residue at the non-reducing end. When the reaction of α-glucuronic acid 1-phosphate (GlcA-1-P) as a glycosyl donor and

An Escherichia coli clone was detected in a Clostridium butyricum NCIMB 7423 plasmid library capable of degrading soluble amylose. Deletion subcloning of its recombinant plasmid indicated that the gene(s) responsible for amylose degradation was localized on a 1.8 kb NspHI-Scal fragment. This region