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At least 19 recordsLinked to original sources
PubMed1978

Hydrolysis of aryl beta-maltotriosides by sweet potato beta-amylase and soybean beta-amylase.

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 soybean beta-amylase [EC 3.2.1.2, alpha-1,4-D-glucan maltohydrolase] were also studied at pH 5.4 and 25 degrees C. It was found that the aryl beta-maltotriosides were preferentially hydrolyzed into maltose and aryl beta-D-glucosides by both beta-amylases. The Michaelis constant Km and the molecular activity ko were determined for the hydrolyses of these maltotriosides and compared with those of maltotriose and maltotetraose. Aryl beta-maltotriosides were more rapidly hydrolyzed than maltotriose by a factor of 30--80, and more slowly hydrolyzed than maltotetraose by a factor of 10--30, depending on the kinds of substituents. The rapid hydrolysis of aryl beta-maltotrioside as compared with maltotriose may be due to the interaction of an aryl group with the subsite of beta-amylase. This is in contrast with glucoamylase [EC 3.2.1.3, alpha-1,4-D-glucan glucohydrolase] of Rhizopus niveus-catalyzed hydrolysis of phenyl beta-maltoside, whose phenyl group does not interact so much with the subsite of the enzyme.

Amylases↗
PubMed1979

Kinetic study of soybean beta-amylase. The effect of pH.

1) Beta-Amylase [EC 3.2.1.2] was prepared from defatted hawk eye soybean flour. The enzyme concentration dependence of the initial velocity for the hydrolytic reaction was investigated at pH 5.4 in the range of the enzyme concentration from 6.6 x 10(-10) M to 5.0 x 10(-6) M. It was found that the initial velocity was proportional to the enzyme concentration in this range. 2) The hydrolyses of maltodextrin (DPn = 74.4) and soluble starch catalyzed by soybean beta-amylase were investigated in the pH range from 3.0 to 9.1 at 25 degrees C, and the Michaelis constant, Km, and the maximum velocity, V, for each substrate were determined at each pH. The pH-rate profile showed a bell-shaped curve, and the pH "optimum" was at 5.85. From Dixon plots of V and V/Km, the pK values were found to be 3.5 and 8.2 for the free enzyme, and 3.5 and 8.5 for the enzyme-substrate complex. The pH-rate profile in the presence of 25% methanol (v/v) was also obtained at alkaline pH. The pKe values were the same as those in the absence of methanol. Based on these results, it was estimated that the ionizable acidic group was an amino group and the basic group was a carboxyl one.

Amylases↗
PubMed1977

[Changes in the activity and tertiary structure of beta-amylase from wheat seeds under the effect of salts].

Changes are observed of 1-anylinonaphtalene-8-sulphonate probe fluorescence intensity, connected with beta-amylase in the presence of Ca(NO3)2, Mg(NO3)2, KNO3, NH4NO3 and (NH4)2SO4 at a concentration range within 10(-4)--1 M. Considerable decrease of the fluorescence intensity was observed under the addition of all the salts mentioned at concentration of 10(-3)--10(-4) M. A quantum yield increase of probe fluorescence was noted for Mg(NO3)2 (10(-4) M). High concentrations of Ca(NO3)2 and Mg(NO3)2 (0.25--1 M) also resulted in a sharp increase of the fluorescence intensity. Changes of beta-amylase activity took place simultaneously. The changes of the enzyme activity are suggested to be due to changes in the conformation of the enzyme protein under the effect of salts.

Amylases↗
PubMed1976

[Mechanism of amylase action on glucoside starch bonds].

Functional groups of glucoamylase and alpha-amylase from Asp. awamori, alpha-amylase from Asp. oryzae and alpha- and beta-amylases from barley malt are identified. Kinetic curves of the activity dependency on pH, values of ionization heats and photooxidative inactivation draw to the conclusion that carboxyl-imidazole system enters into the active site of the enzymes. A hypothetic mechanism of hydrolysis of alpha-1,4-glucoside bond in starch molecule by alpha- and beta-amylases and of alpha-1,4- and alpha-1,6-glucoside bonds by glucoamylase is given. A theory of induced correspondence of enzyme and substrate satisfactorily explains the specificity of the enzyme action and the cause of complete starch convertion into glucose under glucoamylase action and of terminal starch hydrolysis by alpha- and beta-amylases.

Amylases↗
PubMed1978

Pathway of starch breakdown in photosynthetic tissues of Pisum sativum.

1. The aim of this work was to discover the pathway of starch breakdown in the photosynthetic tissues of Pisum sativum. 2. Measurements of the starch in the leaves of plants grown in photoperiods of 12 or 18 h showed that starch, synthesized in the light, was rapidly metabolized in the dark at rates of 0.04--0.06 mumol glucose/min per g fresh weight. 3. The maximum catalytic activities of alpha-amylase, beta-amylase, hexokinase, alpha-glucan phosphorylase and phosphoglucomutase in extracts of leaves showed no diurnal variation in either photoperiod, and exceeded estimates of the rate of net starch breakdown in the dark. 4. Studies with intact chloroplasts, isolated from young shoots and from leaves, indicated that pea chloroplasts do not contain significant activities of alpha-amylase, beta-amylase and hexokinase, although some of the latter may be attached to the outside of the chloroplast envelope. These studies also showed that pea chloroplasts contained sufficient alpha-glucan phosphorylase and phosphoglucomutase to mediate the observed rates of starch breakdown. 5. It is proposed that starch breakdown in pea chloroplasts is phosphorolytic.

Chloroplasts↗
PubMed1975

Purification and some properties of a novel maltohexaose-producing exo-amylase from Aerobacter aerogenes.

Maltohexaose producing amylase (EC 3.2.1.-) is the fourth known exo-amylase, the three previously known being glucoamylase, beta-amylase and Pseudomonas stutzeri maltotetraose producing amylase. The enzyme after release from Aerobacter aerogenes cells by 0.1% sodium lauryl sulfate extraction was purified by ammonium sulfate precipitation, DEAE-Sephadex column chromatography and Sephadex G-100 gel filtration to 80-fold of the original sodium lauryl sulfate extract activity, It gave a single band on disc electrophoresis, and the molecular weight by gel filtration was 54 000. This amylase showed maximal activity at 50 degrees C and pH 6.80. The pH stability range was relatively wide, the enzyme retaining more than 90% of its initial activity in the range of 6.50-9.0. 80% of the activity was retained after 15 min at 50 degrees C. This enzyme produced maltohexaose from starch, amylose and amylopectin by exo-attack, but did not act on alpha- or beta-cyclodextrin, pullulan or maltohexaitol. Also the enzyme acted on beta-limit dextrins of amylopectin and glycogen to form branched oligosaccharides. The unusual reaction of this enzyme on beta-limit dextrin is discussed from the standpoint of the stereochemistry of 1,4-alpha- and 1,6-alpha-glucosidic bonds. This is the anomalous amylase for which it is recognized that 1,6-alpha-glucosidic linkages in the substrates can mimic the effect of 1,4-alpha-bonds, as previously observed in pseudo-priming reactions of E. coli phosphorylase.

Amylases↗
PubMed1978

Biosynthesis of glycogen in Neurospora crassa. Purification and properties of the UDPglucose:glycogen 4-alpha-glucosyltransferase.

The Neurospora crassa glycogen synthase (UDPglucose:glycogen 4-alpha-glucosyltransferase, EC 2.4.1.11) was purified to electrophoretic homogeneity by a procedure involving ultracentrifugation, DEAE-cellulose column chromatography, (NH4)2SO4 fractionation and 3-aminopropyl-Sepharose column chromatography. The final purified enzyme preparation was almost entirely dependent on glucose-6-P and had a specific activity of 6.9 units per mg of protein. The subunit molecular weight of the glycogen synthase was determined by electrophoresis in sodium dodecyl sulfate-polyacrylamide gel to be 88 000--90 000. The native enzyme was shown to have a molecular weight of 270 000 as determined by sucrose density gradient centrifugation. Thus, the glucose-6-P-dependent form of the N. crassa glycogen synthase can exist as trimer of the subunit. Limited proteolysis with trypsin or chymotrypsin converted the glucose-6-P-dependent form of the enzyme into an apparent glucose-6-P-independent form. The enzyme was shown to catalyze transfer of glucose from UDPglucose to glycogen as well as to its phosphorylase limit dextrin, but not to its beta-amylase limit dextrin. Moreover, glucose, maltose and maltotriose were not active as acceptors.

Cations, Divalent↗
PubMed2025

Role of functional genes for seed vigor related traits through genome-wide association mapping in finger millet (Eleusine coracana L. Gaertn.).

Finger millet (Eleusine coracana (L.) Gaertn.) is a calcium-rich, nutritious and resilient crop that thrives even in harsh environmental conditions. In such ecologies, seed longevity and seedling vigor are crucial for sustainable crop production amid climate change. The current study explores the genetics of accelerated aging on seed longevity traits across 221 diverse accessions of finger millet through genome-wide association approach (GWAS). A significant variation was identified in germination percentage, germination rate indices, mean germination time, seedling vigor indices and dry weight upon aging treatment. GWAS model from 11,832 high-quality SNPs identified through Genotyping-by-Sequencing (GBS) approach produced 491 marker-trait associations (MTAs) for 27 traits, of which 54 were FDR-corrected. A pleiotropic SNP, FM_SNP_9478 identified on chromosome 7B was associated with the traits viz., germination after aging, germination index after aging and their relative measures. Functional annotation revealed DET1 and expansin-A2 influenced seed coat integrity, critical for germination and aging resilience. Probable protein phosphatase 2C3 and piezo-type ion channels contributed to mechanical sensing and stress adaptation in seeds. Beta-amylase and acetyl-CoA carboxylase 2 were identified for seed metabolism and stress response. These insights lay the framework for targeted breeding efforts to improve seed quality and resilience under diverse production conditions.

Eleusine↗
PubMed1978

[Effect of physical and chemical factors on the antigenic activity of the cell walls of Brucella abortus 99].

Studied was the effect of some physical and chemical factors--heating, acidity, treatment with ultraviolet rays, and enzyme treatment--on the activity of the Brucella abortus 99 cell wall antigen. The activity of the antigen was determined through the microreaction of complement-fixing after Kolmer. It was found that the antigen was most sensitive to acid treatment and treatment with ultraviolet rays, and was more slightly sensitive to the effect of alkaline agents and pronase. Besides, the antigen proved heat-resistant and did not lose its activity after treatment with trypsin and alph- and beta-amylase. The chemical nature of the epitopes (the determinant groups), substantiating the activity of the antigen is briefly discussed.

Amylases↗
PubMed1978

Clinical evaluation of the pancreatitis-like isoamylase pattern in normal persons.

Amylase isoenzyme analysis of serum and urine has been performed in 4001 normal persons and 500 patients with various disease using electrophoresis on thin layer polyacrylamide gel. Although elevation of amylase activity in amylase-1 and 2 has been reported to be the specific findings in patients with pancreatitis, 1.69% of normal persons had an elevated Amylase-2(named "Dominant Amylase-2") up to the same levels as major isoenzymes (Amylase-1 and 3), along with Amylase-1. Pedigree study confirmed an autosomal dominant mode of inheritance for Dominant Amylase-2. Knowledge of the genetic polymorphism is of importance in clinical assessment of amylase isoenzymes in patients having an elevated Amylase-2 suggestive of pancreatitis. Predominance of the pancreatic components in serum and urine has been revealed to be a specific index of pancreatic involvement. However, the existecne of an inherited trait of pancreatitis-like isoamylase pattern in healthy individuals must be borne in mind. On the basis of the present study, it may be concluded that a rise in the pancreatic type isoenzymes may not necessarily indicate underlying pancreatitis, especially in the absence of elevated amylase and lipase levels.

Acute Disease↗
PubMedDate not supplied

[Immunochemical characterization of alpha-amylases in wheat seeds at different ontogenical steps (author's transl)].

Protein extracts of wheat seeds taken at an early stage of development, at maturation and after seven days of germination were investigated by using immunochemical techniques with immune sera prepared against alpha-amylases purified from developing seeds and alpha-amylases purified from germinated seeds. After immunochemical analyses carried out in agarose gel, alpha-amylase characterization was performed by using beta-limit dextrin followed by iodine staining. Detection of three antigenic alpha-amylases separated by agarose immunoelectrophoretic analysis at pH 8.6 and called I, II, III from the anode to the cathode, as well as an antigenical relationship between the anodic enzymes I and II were confirmed. Three constituents in I and four in II were further distinguished by using long duration electrophoresis in agarose gel. The immune sera reacted with all of these constituents. Thus with these immune sera a quantitative determination of all anodic alpha-amylase proteins can be attempted as quantitation of two antigens. During this identification consitutents with a apparent activity on beta-limit dextrin but delivering incomplete unstained substrate were detected. These constituents found in developing seeds have electrophoretic mobility close to that of constituents I but differ antigenically from alpha-amylases I and II. Combination of rocket-line-immunoelectrophoresis and alpha-amylase characterization reaction on precipitin bands was developed for comparing amounts of each of three alpha-amylase antigens in different seed extracts. The use of this technique for quantitating at the same time two antigen groups having a certain cross reactivity is discussed. Preliminary results of quantitative study on each of these antigen in developing, mature and germinating seeds are reported.

Amylases↗
PubMed1978

Nutritional and toxicological properties of some raw and modified starches.

Several food additives, including some raw and chemically modified starches, sorbitol and maltitol, cause caecal enlargement when fed to rodents. The onset of caecal enlargement is rapid and it is reversible when the additive is withdrawn. This poses problems in the safety evaluation of such additives, both in relation to the significance of the caecal enlargement and to the associated effects on food efficiency and nitrogen balance. The mechanisms of causation of caecal enlargement have been studied and will be discussed with particular reference to resistance of starches to enzymic hydrolysis, changes in intestinal microflora, osmotic load in the caecum, cell hyperplasia and rate of turnover of mucosal cells. Where deaths occur, these appear to be due to secondary effects such as impaired resporatory function.

Animals↗