scholarly journals A novel alpha-glucosidase from the moss Scopelophila cataractae.

2007 ◽  
Vol 54 (2) ◽  
pp. 401-406 ◽  
Author(s):  
Yoshiki Yamasaki ◽  
Susumu Nakashima ◽  
Haruyoshi Konno
Keyword(s):  
Phosphate Buffer ◽  
Soluble Starch ◽  
Ms Medium ◽  
Starch Digestion ◽  
Soluble Extract ◽  
Debranching Enzyme ◽  
Successive Extraction ◽  
Isoelectric Points ◽  
Alpha Amylase Inhibitor ◽  
Alpha Glucosidase

Scopelophila cataractae is a rare moss that grows on copper-containing soils. S. cataractae protonema was grown on basal MS medium containing copper. A starch-degrading activity was detected in homogenates of the protonema, after successive extraction with phosphate buffer and buffer containing 3 M LiCl. Buffer-soluble extract (BS) and LiCl-soluble extract (LS) readily hydrolyzed amylopectin to liberate only glucose, which shows that alpha-glucosidase (EC 3.2.1.20) in BS and LS hydrolyzed amylopectin. The K(m) value of BS for maltose was 0.427. The K(m) value of BS for malto-oligosaccharide decreased with an increase in the molecular mass of the substrate. The value for maltohexaose was 0.106, which is about four-fold lower than that for maltose. BS was divided into two fractions of alpha-glucosidase (BS-1 and BS-2) by isoelectric focusing. The isoelectric points of these two enzymes were determined to be 4.36 (BS-1) and 5.25 (BS-2) by analytical gel electrofocusing. The two enzymes readily hydrolyzed malto-oligosaccharides. The two enzymes also hydrolyzed amylose, amylopectin and soluble starch at a rate similar to that with maltose. The two enzymes readily hydrolyzed panose to liberate glucose and maltose (1 : 1), and the K(m) value of BS for panose was similar to that for maltotriose, whereas the enzymes hydrolyzed isomaltose only weakly. With regard to substrate specificity, the two enzymes in BS are novel alpha-glucosidases. The two enzymes also hydrolyzed beta-limit dextrin, which has many alpha-1,6-glucosidic linkages near the non-reducing ends, more strongly than maltose, which shows that they do not need a debranching enzyme for starch digestion. The starch-degrading activity of BS was not inhibited by p-chloromercuribenzoic acid or alpha-amylase inhibitor. When amylopectin was treated with BS and LS in phosphate buffer, pH 6.0, glucose, but not glucose-1-phosphate, was detected, showing that the extracts did not contain phosphorylase but did contain an alpha-glucosidase. These results show that alpha-glucosidases should be capable of complete starch digestion by themselves in cells of S. cataractae.

scholarly journals QUANTITATIVE AND HISTOCHEMICAL STUDIES ON THE DESORPTION AND READSORPTION OF ALDOLASE IN CROSS-STRIATED MUSCLE

1969 ◽  
Vol 17 (5) ◽  
pp. 314-320 ◽  
Author(s):  
H. ARNOLD ◽  
J. NOLTE ◽  
D. PETTE
Keyword(s):  
Enzyme Activity ◽  
Actin Filaments ◽  
Phosphate Buffer ◽  
Striated Muscle ◽  
Psoas Muscle ◽  
Histochemical Staining ◽  
Intracellular Location ◽  
Successive Extraction ◽  
Complete Extraction

Complete extraction of aldolase from minced rabbit psoas muscle was achieved by successive extraction steps in 0.1 M phosphate buffer. Aldolase was then readsorbed quantitatively to the depleted myofibrils. Extraction, readsorption and a final redsorption of the enzyme were followed quantitatively by enzyme activity determinations and qualitatively by histochemical staining of aldolase. The intracellular location of the readsorbed enzyme was found to be identical with that of aldolase in native muscle. In both cases, aldolase was localized within the isotropic bands. These results as well as the previously demonstrated binding of the enzyme to F-actin suggest that aldolase is located within the interfilamentary sarcoplasm of the isotropic bands and is probably also bound in vivo to the actin filaments.

A New Saccharogenic Micromethod for Measurement of Amylase Activity in Biological Fluids

1970 ◽  
Vol 16 (4) ◽  
pp. 300-304 ◽  
Author(s):  
Klaus Lorentz ◽  
Detlef Oltmanns
Keyword(s):  
Standard Deviation ◽  
Blood Donors ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Biological Fluids ◽  
Soluble Starch ◽  
Starch Digestion ◽  
Triphenyltetrazolium Chloride ◽  
Serum Amylase Activity ◽  
Apparently Healthy

Abstract To determine serum amylase activity we have quantitatively measured the glucose and maltose hydrolyzed from soluble starch by colorimetrically measuring the reduction of colorless triphenyltetrazolium chloride to a red formazan, which is dissolved in methanol. The method is suitable for use with microsamples of all biological fluids, and is specific for the final products of starch digestion. Values found for sera from 55 apparently healthy blood donors ranged from 0.15 to 1.55 (mean, 0.83; standard deviation, ±0.4) mg of glucose per ml per h, corresponding to 7.5 to 78 Somogyi units.

scholarly journals Evaluation of Ant‐Lion Larvae Extract As Alpha‐Glucosidase and Alpha‐Amylase Inhibitor

2019 ◽  
Vol 33 (S1) ◽  
Author(s):  
Muinat Moronke Adeyanju ◽  
Omolayo Omobolawa OLANIYI ◽  
Olashile Fatimat RASAK ◽  
Oyewale Oluwapelumi ADEOSUN ◽  
Joseph Senu ASHIDI ◽  
...  
Keyword(s):  
Alpha Amylase ◽  
Amylase Inhibitor ◽  
Alpha Amylase Inhibitor ◽  
Ant Lion ◽  
Alpha Glucosidase

scholarly journals Development of a Novel Series of Anticancer and Antidiabetic: Spirothiazolidines Analogs

Molecules ◽  
2019 ◽  
Vol 24 (13) ◽  
pp. 2511 ◽  
Author(s):  
Eman M. Flefel ◽  
Walaa I. El-Sofany ◽  
Reem A.K. Al-Harbi ◽  
Mahmoud El-Shahat
Keyword(s):  
Positive Control ◽  
The Other ◽  
Liver Carcinoma ◽  
Anticancer Activities ◽  
Alpha Amylase Inhibitor ◽  
Nitrogen Nucleophiles ◽  
Active Methylene ◽  
Alpha Glucosidase ◽  
Mcf 7

4-(4-Aminophenyl)-1-thia-4-azaspiro[4.5]decan-3-one 1 was prepared and allowed to react with nitrogen nucleophiles to give the corresponding hydrazones 2–4. Further, compound 1 underwent diazotization and afforded the parallel hydrazono derivative 5; moreover, compound 1 refluxed with active methylene derivatives yielded the corresponding aminospirothiazolo pyridine–carbonitrile derivative 6 and spirothiazolopyridinone–carbonitrile derivative 7. Condensation of spirothiazolidine 1 with 4-chlorobenzaldehyde gave the corresponding spiro arylidiene derivative 8, which was utilized as a component of Micheal addition to react with excess of nitrogen nucleophiles to yield novel ring frameworks 4-(3′-(4-chlorophenyl)–spiro [cyclohexane-1,5′-pyrazolo[3,4-d]thiazol]-6′(1′H)-yl)aniline (9) and 4-(3′-(4-chlorophenyl)-6′H- spiro[cyclohexane-1,5′-thiazolo[5,4-d]isoxazol]-6′-yl)aniline (10). Finally, when spirothiazolo pyridinone–carbonitrile derivative 7 sodium salt generated in situ was reacted with different alkyl halides, it produced the corresponding N-derivatives 12–16. Three compounds, 6, 14, and 16, showed high significantly anticancer activities compared with Doxorubicin® (positive control) against human breast carcinoma (MCF-7) and human liver carcinoma (HepG-2) cell lines. On the other hand, compounds 6 and 9 showed higher therapeutic indices for both of alpha-amylase inhibitor and alpha-glucosidase inhibitor than the other tested compounds compared with the antidiabetic Acarbose (positive control).

Digestive α-amylases from Tecia solanivora larvae (Lepidoptera: Gelechiidae): response to pH, temperature and plant amylase inhibitors

2008 ◽  
Vol 98 (6) ◽  
pp. 575-579 ◽  
Author(s):  
A. Valencia-Jiménez ◽  
J.W. Arboleda V ◽  
A. López Ávila ◽  
M.F. Grossi-de-Sá
Keyword(s):  
Amylase Activity ◽  
Insect Pest ◽  
Biochemical Properties ◽  
Alpha Amylase ◽  
Isoelectric Points ◽  
Optimum Ph ◽  
Tecia Solanivora ◽  
Alpha Amylase Inhibitor ◽  
Amylase Inhibitors ◽  
Genetically Modified Potatoes

AbstractThe biochemical properties of the digestive alpha-amylase from Tecia solanivora larvae, an important and invasive insect pest of potato (Solanum tuberosum), were studied. This insect has three major digestive α-amylases with isoelectric points 5.30, 5.70 and 5.98, respectively, which were separated using native and isoelectric focusing gels. The alpha-amylase activity has an optimum pH between 7.0 and 10.0 with a peak at pH 9.0. The enzymes are stable when heated to 50°C and were inhibited by proteinaceous inhibitors from Phaseolus coccineus (70% inhibition) and P. vulgaris cv. Radical (87% inhibition) at pH 6.0. The inhibitors present in an amaranth hybrid inhibited 80% of the activity at pH 9.0. The results show that the alpha-amylase inhibitor from amaranth seeds may be a better candidate to make genetically-modified potatoes resistant to this insect than inhibitors from common bean seeds.

Purification of extracellular amylolytic enzymes from the thermophilic fungus Thermomyces lanuginosus

1988 ◽  
Vol 34 (3) ◽  
pp. 218-223 ◽  
Author(s):  
Bo Jensen ◽  
Jorgen Olsen ◽  
Knud Allermann
Keyword(s):  
Molecular Weight ◽  
Ion Exchange ◽  
Soluble Starch ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Thermomyces Lanuginosus ◽  
Amylolytic Enzymes ◽  
Molecular Weights ◽  
Isoelectric Points ◽  
Hydrolysis Of

When grown in static culture it appears as if Thermomyces lanuginosus has a biphasic secretion of the extracellular starch-degrading activity. This could be due to the presence of at least two different amylases. By ion-exchange chromatography on DEAE-Trisacryl an α-amylase (EC 3.2.1.1) and a glucoamylase (EC 3.2.1.3) were separated and purified from the extracellular protein from 14-day-old static cultures grown on soluble starch. The hydrolysis of soluble starch by the purified glucoamylase resulted in only glucose as the end product, whereas the α-amylase gave maltose as the smallest end product. The molecular weights and isoelectric points of the enzymes were for glucoamylase 70 000 – 76 000 and pH 4.0, and for α-amylase 54 000 – 57 000 and pH 3.4. An α-glucosidase (EC 3.2.1.20) with a molecular weight of 44 000 – 48 000 and an isoelectric point at pH 3.8 was eluted close to the α-amylase fraction on the DEAE-Trisacryl column.

The in vitro growth and metabolism of Acer saccharum tissue

1971 ◽  
Vol 49 (4) ◽  
pp. 495-500 ◽  
Author(s):  
Martin C. Mathes ◽  
Mariafranca Morselli ◽  
J. W. Marvin
Keyword(s):  
Acer Saccharum ◽  
Sugar Maple ◽  
Culture Medium ◽  
Basal Medium ◽  
Soluble Starch ◽  
Defined Medium ◽  
Tissue Growth ◽  
Starch Digestion ◽  
Callus Tissues

Isolated sugar maple callus was grown on defined medium containing 0.2 kinetin and 2.0 ppm indoleacetic acid. Selected components of the basal medium were varied but did not result in increased tissue growth. The presence of 1, 5, or 25 ppm gibberellic acid in the culture medium did not increase the secretion of starch digesting materials by the tissue. The diameter of the starch digestion zone was not influenced by changing the acidity of the medium in the range of pH which supported tissue growth. The ability of isolated callus tissues from various species to digest extracellular starch was examined. It was found that equal amounts of various tissues do not possess an equal capacity for the in vitro secretion of extracellular materials, most probably enzymes, into the culture medium. It was found that isolated sugar maple tissue metabolized sucrose, galactose, and cellobiose while mannose and rhamnose were not used.Isolated sugar maple tissue which had been subcultured on the same medium for a long period was found to undergo nutritional changes which enabled the tissue to adapt to the medium. The starch-digestion enzyme activity of the tissue was found to increase when sugar maple tissue was placed on soluble starch medium.

scholarly journals Maltose production from soluble starch by .BETA.-amylase and debranching enzyme immobilized on ceramic monolith.

1988 ◽  
Vol 14 (3) ◽  
pp. 288-294 ◽  
Author(s):  
Fumihide Shiraishi ◽  
Koei Kawakami ◽  
Tsuyoshi Kojima ◽  
Akio Yuasa ◽  
Koichiro Kusunoki
Keyword(s):  
Soluble Starch ◽  
Debranching Enzyme
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