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alpha glucan/dacsa
L'enllaç es desa al porta-retalls
12 resultats
Purification and Properties of Mesophyll and Bundle Sheath Cell alpha-Glucan Phosphorylases from Zea mays L. : Equivalence of the Enzymes with the Cytosol and Plastid Phosphorylases from Spinach.
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Two major alpha-glucan phosphorylases (I and II) from leaves of the C(4) plant corn (Zea mays L.) were previously shown to be compartmented in mesophyll and bundle sheath cells, respectively (C Mateyka, C Schnarrenberger 1984 Plant Sci Lett 36: 119-123). The two enzymes were separated by
Purification and Partial Characterization of a Glucan Containing Indole-3-acetic Acid.
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The "bound auxin" of Zea mays, first described by Berger and Avery (Amer. J. Bot. 1944; 31: 199-203) has been purified and partially characterized. It is an indole-3-acetic acid-containing, high molecular weight, lipophilic cellulosicglucan. The indole-3-acetic acid is in ester linkage as evidenced
Identification of Mutator insertional mutants of starch-branching enzyme 1 (sbe1) in Zea mays L.
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Starch-branching enzymes (SBE) alter starch structure by breaking an alpha-1,4 linkage and attaching the reducing end of the new chain to a glucan chain by an alpha 1,6 bond. In maize, three isoforms of SBE have been identified. In order to examine the function of the SBEI isoform, a
High level accumulation of alpha-glucan in maize kernels by expressing the gtfD gene from Streptococcus mutans.
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Glucosyltransferases (GTFs, EC.2.4.1.5) are bacterial enzymes that catalyze the polymerization of glucose residues from sucrose, leading to the production of high molecular weight glucan with alpha-1,3 /alpha-1,6 linkages. Such glucans, with many potential food and industrial applications, do not
Functional interactions between heterologously expressed starch-branching enzymes of maize and the glycogen synthases of Brewer's yeast.
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Starch-branching enzymes (SBEs) catalyze the formation of alpha(1-->6) glycoside bonds in glucan polymers, thus, affecting the structure of amylopectin and starch granules. Two distinct classes of SBE are generally conserved in higher plants, although the specific role(s) of each isoform in
A partial characterization of an autolytically solubilized cell wall glucan.
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Incubation of purified cell wall fragments from corn (Zea mays) coleoptiles results in solubilization of some of the wall dry matter. The portion of the weight loss due to enzymatic autolysis is due mainly to solubilization of a glucan and, to a small extent, to liberation of free glucose. No other
Transcriptome wide identification and characterization of starch branching enzyme in finger millet.
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Starch-branching enzymes (SBEs) are one of the four major enzyme classes involved in starch biosynthesis in plants and play an important role in determining the structure and physical properties of starch granules. Multiple SBEs are involved in starch biosynthesis in plants. Finger millet is calcium
Identification of Mutator insertional mutants of starch-branching enzyme 2a in corn.
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Starch-branching enzymes (SBE) break the alpha-1,4 linkage of starch, re-attaching the chain to a glucan chain by an alpha-1,6 bond, altering starch structure. SBEs also facilitate starch accumulation by increasing the number of non-reducing ends on the growing chain. In maize (Zea mays), three
Selective Knockdowns in Maize by Sequence-Specific Protein Aggregation.
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Protein aggregation is determined by 5-15 amino acids peptides of the target protein sequence, so-called aggregation-prone regions (APRs) that specifically self-associate to form β-structured inclusions. The presence of APRs in a target protein can be predicted by a dedicated algorithm, such as
Sequence-Specific Protein Aggregation Generates Defined Protein Knockdowns in Plants.
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Protein aggregation is determined by short (5-15 amino acids) aggregation-prone regions (APRs) of the polypeptide sequence that self-associate in a specific manner to form β-structured inclusions. Here, we demonstrate that the sequence specificity of APRs can be exploited to selectively knock down
A thermostable glucoamylase from Bispora sp. MEY-1 with stability over a broad pH range and significant starch hydrolysis capacity.
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BACKGROUND
Glucoamylase is an exo-type enzyme that converts starch completely into glucose from the non-reducing ends. To meet the industrial requirements for starch processing, a glucoamylase with excellent thermostability, raw-starch degradation ability and high glucose yield is much needed. In
Starch Synthetase, Phosphorylase, ADPglucose Pyrophosphorylase, and UDPglucose Pyrophosphorylase in Developing Maize Kernels.
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Soluble ADPglucose-alpha-glucan 4-alpha-glucosyltransferase (starch synthetase), ADPglucose pyrophosphorylase, UDPglucose pyrophosphorylase and phosphorylase were assayed in extracts from developing kernels of maize (Zea mays). Normal, waxy and amylose-extender maize at stages of development ranging
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