cystine/بطاطس

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Effect of cysteine and cystine addition on sensory profile and potent odorants of extruded potato snacks.

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Aromas generated in extruded potato snacks without and with addition of 0.25, 0.5, and 1% (w/w) of flavor precursors, cysteine and cystine, were compared and evaluated by descriptive sensory profiling. The results showed that high addition of cysteine (0.5 and 1%) resulted in the formation of

Biochemical and MALDI-TOF Mass Spectrometric Characterization of a Novel Native and Recombinant Cystine Knot Miniprotein from Solanum tuberosum subsp. andigenum cv. Churqueña.

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Cystine-knot miniproteins (CKMPs) are an intriguing group of cysteine-rich molecules that combine the characteristics of proteins and peptides. Typically, CKMPs are fewer than 50 residues in length and share a characteristic knotted scaffold characterized by the presence of three intramolecular

Digestion of wheat gluten and potato protein by the preruminant calf: digestibility, amino acid composition and immunoreactive proteins in ileal digesta.

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Three milk substitute diets, in which the protein was either provided exclusively by skim milk powder or partially (52%) substituted by a native wheat gluten or a potato protein concentrate, were given to intact or ileo-caecal cannulated preruminant calves. The apparent faecal nitrogen digestibility

Amino acid sequence of an active fragment of potato proteinase inhibitor IIa.

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The complete amino acid sequence of an active fragment of potato proteinase inhibitor IIa has been established by the Edman degradation procedure and the carboxypeptidase technique. Sequence analyses were carried out on the reduced and carboxymethylated active fragment and its tryptic peptides. To

Structure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 A resolution.

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A low molecular weight protein inhibitor of serine proteinases from Russet Burbank potato tubers, polypeptide chymotrypsin inhibitor-1 (PCI-1), has been crystallized in complex with Streptomyces griseus proteinase B (SGPB). The three-dimensional structure of the complex has been solved at 2.1 A

Naturally occurring protein crystals in the potato : inhibitor of papain, chymopapain, and ficin.

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Protein crystals isolated from potato tubers were found to consist of a proteinase inhibitor active against the cysteine proteinases papain, chymopapain, and ficin. The molecular weight as determined by gel filtration at pH 4.3 or by gel electrophoresis in the presence of dodecylsulfate was 80

Homologous inhibitors from potato tubers of serine endopeptidases and metallocarboxypeptidases.

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A potent polypeptide inhibitor of chymotrypsin has been purified from Russett Burbank potatoes. The inhibitor has no effect on bovine carboxypeptidases A or B but exhibits homology with a carboxypeptidase inhibitor that is also present in potato tubers. The chymotrypsin inhibitor has a molecular

The disulfide folding pathway of potato carboxypeptidase inhibitor.

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Potato carboxypeptidase inhibitor (PCI) contains 39 amino acids and three disulfides. Reduced and denatured PCI refolds spontaneously in vitro to regain its native structure. The folding pathway of a recombinant form of this protein has been elucidated by structural analysis and stop/go folding

The purification and properties of the lectin from potato tubers, a hydroxyproline-containing glycoprotein.

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1. Potato lectin has been purified and shown to be a glycoprotein containing about 50% of carbohydrate. Most of the sugar residues (92%) are arabinose; small amounts of galactose, glucose and glucosamine are also present. 2. The most abundant amino acid is hydroxyproline (16% of the residues), 11.5%

Amino acid sequence of an active fragment of potato proteinase inhibitor IIb.

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The amino acid sequence of an active fragment of potato proteinase inhibitor IIb was determined by the Edman degradation procedure and the carboxypeptidase technique. Analyses were carried out on peptides derived from the reduced and carboxymethylated active fragment by digestion with trypsin and

Reduction and carboxamidomethylation of the single disulfide bond of proteinase inhibitor I from potato tubers. Effects on stability, immunological properties, and inhibitory activities.

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The single disulfide bond in potato Inhibitor I protomers (Mr = 8,000) was reduced and alkylated in the absence of denaturants to the carboxamidomethyl cysteine derivative. Two half-cystines per mol of inhibitor protomer were modified as determined by (a) loss of two sulfhydryl groups per reduced

Effects of sulphur, nitrogen, phosphorus, potassium, and water stress on dietary fibre fractions, starch, amino acids and on the biological value of potato protein.

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In pot experiments with greatly differing rates of N, P, K, and S, and 3 levels of water, dry matter (DM) yields of tubers varied from 28 to 454 g/pot. Especially P-, K- and S-deficiency reduced the starch content of boiled potatoes, from P from 74 to 59% in DM. S-deficiency increased soluble,

Effects of oven-drying tubers of two high-protein sweet potato varieties at different temperatures on their feeding value in broilers.

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1. Unpeeled tubers from 2 high-protein varieties of sweet potato (white-fleshed Bosbok, and orange-fleshed Carmel) were chipped and oven-dried at 40, 60, or 80 degrees C, to examine the effects on nutritive value. The dried ground chips were substituted for maize at 500 g/kg and the diets fed to

Plant cystine-knot peptides: pharmacological perspectives.

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Cystine-knot miniproteins are a class of 30-50 amino acid long peptides widespread in eukaryotic organisms. Due to their very peculiar three-dimensional structure, they exhibit high resistance to heat and peptidase attack. The cystine-knot peptides are well represented in several plant species

Potato lectin: a three-domain glycoprotein with novel hydroxyproline-containing sequences and sequence similarities to wheat-germ agglutinin.

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Potato (Solanum tuberosum) tuber lectin is a chitin-binding, hydroxyproline-rich glycoprotein, which may be involved in the defence mechanism of the plant. We had previously obtained evidence that it consists of at least two very dissimilar domains. The aim was to use a combination of accurate

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