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Thermodynamic and activation parameters for the hydrolysis of amylose with Bacillus alpha-amylases in a diluted anionic surfactant solution.

Journal of bioscience and bioengineering

Tanaka A, Hoshino E.
PMID: 16233236
J Biosci Bioeng. 2002;93(5):485-90. doi: 10.1016/s1389-1723(02)80096-2.

The effects of an anionic surfactant, sodium dodecyl sulfate (SDS), on the kinetic behavior in the hydrolysis of amylose with two bacterial alpha-amylases from Bacillus amyloliquefaciens and B. licheniformis were studied. The catalytic rates of both amylases in the...

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Tanaka A, Hoshino E. Thermodynamic and activation parameters for the hydrolysis of amylose with Bacillus alpha-amylases in a diluted anionic surfactant solution. J Biosci Bioeng. 2002;93(5):485-90doi: 10.1016/s1389-1723(02)80096-2.
Tanaka, A., & Hoshino, E. (2002). Thermodynamic and activation parameters for the hydrolysis of amylose with Bacillus alpha-amylases in a diluted anionic surfactant solution. Journal of bioscience and bioengineering, 93(5), 485-90. https://doi.org/10.1016/s1389-1723(02)80096-2
Tanaka, Atsushi, and Hoshino, Eiichi. "Thermodynamic and activation parameters for the hydrolysis of amylose with Bacillus alpha-amylases in a diluted anionic surfactant solution." Journal of bioscience and bioengineering vol. 93,5 (2002): 485-90. doi: https://doi.org/10.1016/s1389-1723(02)80096-2
Tanaka A, Hoshino E. Thermodynamic and activation parameters for the hydrolysis of amylose with Bacillus alpha-amylases in a diluted anionic surfactant solution. J Biosci Bioeng. 2002;93(5):485-90. doi: 10.1016/s1389-1723(02)80096-2. PMID: 16233236.
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On amylolytic enzymes; comparison of the enzymatic action of alpha-amylases from various sources.

Helvetica chimica acta

BERNFELD P, FULD M.
PMID: 18875093
Helv Chim Acta. 1948;31(5):1423-7. doi: 10.1002/hlca.19480310529.

No abstract available.

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BERNFELD P, FULD M. Sur les enzymes amylolytiques; comparaison de l'action enzymatique d' alpha-amylases de diverses provenances. On amylolytic enzymes; comparison of the enzymatic action of alpha-amylases from various sources. Helv Chim Acta. 1948;31(5):1423-7doi: 10.1002/hlca.19480310529.
BERNFELD, P., & FULD, M. (1948). Sur les enzymes amylolytiques; comparaison de l'action enzymatique d' alpha-amylases de diverses provenances. On amylolytic enzymes; comparison of the enzymatic action of alpha-amylases from various sources. Helvetica chimica acta, 31(5), 1423-7. https://doi.org/10.1002/hlca.19480310529
BERNFELD, P, and FULD, M. "Sur les enzymes amylolytiques; comparaison de l'action enzymatique d' alpha-amylases de diverses provenances." On amylolytic enzymes; comparison of the enzymatic action of alpha-amylases from various sources. Helvetica chimica acta vol. 31,5 (1948): 1423-7. doi: https://doi.org/10.1002/hlca.19480310529
BERNFELD P, FULD M. Sur les enzymes amylolytiques; comparaison de l'action enzymatique d' alpha-amylases de diverses provenances. On amylolytic enzymes; comparison of the enzymatic action of alpha-amylases from various sources. Helv Chim Acta. 1948;31(5):1423-7. doi: 10.1002/hlca.19480310529. French. PMID: 18875093.
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Baked-bean waste: a potential substrate for producing fungal amylases.

Applied and environmental microbiology

Hang YD, Woodams EE.
PMID: 16345247
Appl Environ Microbiol. 1977 Jun;33(6):1293-4. doi: 10.1128/aem.33.6.1293-1294.1977.

Baked-bean waste was found to be a favorable substrate for amylase production by Aspergillus foetidus NRRL 337. Under optimum conditions, the yields of alpha-amylase (EC 3.2.1.1) and glucoamylase (EC 3.2.1.3) were 47 and 226 U, respectively, per ml of...

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Hang YD, Woodams EE. Baked-bean waste: a potential substrate for producing fungal amylases. Appl Environ Microbiol. 1977;33(6):1293-4doi: 10.1128/aem.33.6.1293-1294.1977.
Hang, Y. D., & Woodams, E. E. (1977). Baked-bean waste: a potential substrate for producing fungal amylases. Applied and environmental microbiology, 33(6), 1293-4. https://doi.org/10.1128/aem.33.6.1293-1294.1977
Hang, Y D, and Woodams, E E. "Baked-bean waste: a potential substrate for producing fungal amylases." Applied and environmental microbiology vol. 33,6 (1977): 1293-4. doi: https://doi.org/10.1128/aem.33.6.1293-1294.1977
Hang YD, Woodams EE. Baked-bean waste: a potential substrate for producing fungal amylases. Appl Environ Microbiol. 1977 Jun;33(6):1293-4. doi: 10.1128/aem.33.6.1293-1294.1977. PMID: 16345247; PMCID: PMC170875.
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The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86.

BMC research notes

Altenbach SB, Vensel WH, Dupont FM.
PMID: 21774824
BMC Res Notes. 2011 Jul 20;4:242. doi: 10.1186/1756-0500-4-242.

BACKGROUND: Wheat grains accumulate a variety of low molecular weight proteins that are inhibitors of alpha-amylases and proteases and play an important protective role in the grain. These proteins have more balanced amino acid compositions than the major wheat...

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Altenbach SB, Vensel WH, Dupont FM. The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86. BMC Res Notes. 2011;4:242doi: 10.1186/1756-0500-4-242.
Altenbach, S. B., Vensel, W. H., & Dupont, F. M. (2011). The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86. BMC research notes, 4242. https://doi.org/10.1186/1756-0500-4-242
Altenbach, Susan B, et al. "The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86." BMC research notes vol. 4 (2011): 242. doi: https://doi.org/10.1186/1756-0500-4-242
Altenbach SB, Vensel WH, Dupont FM. The spectrum of low molecular weight alpha-amylase/protease inhibitor genes expressed in the US bread wheat cultivar Butte 86. BMC Res Notes. 2011 Jul 20;4:242. doi: 10.1186/1756-0500-4-242. PMID: 21774824; PMCID: PMC3154163.
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beta-Amylases in Cereals : A Study of the Maize beta-Amylase System.

Plant physiology

Laurière C, Doyen C, Thévenot C, Daussant J.
PMID: 16653072
Plant Physiol. 1992 Oct;100(2):887-93. doi: 10.1104/pp.100.2.887.

beta-Amylase of maize (Zea mays L.) caryopses was studied during development and germination by means of enzymic, electrophoretic, and immunochemical techniques. beta-Amylase activity increased during caryopsis development to a maximum value at the beginning of the water content plateau...

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Laurière C, Doyen C, Thévenot C, et al. beta-Amylases in Cereals : A Study of the Maize beta-Amylase System. Plant Physiol. 1992;100(2):887-93doi: 10.1104/pp.100.2.887.
Laurière, C., Doyen, C., Thévenot, C., & Daussant, J. (1992). beta-Amylases in Cereals : A Study of the Maize beta-Amylase System. Plant physiology, 100(2), 887-93. https://doi.org/10.1104/pp.100.2.887
Laurière, C, et al. "beta-Amylases in Cereals : A Study of the Maize beta-Amylase System." Plant physiology vol. 100,2 (1992): 887-93. doi: https://doi.org/10.1104/pp.100.2.887
Laurière C, Doyen C, Thévenot C, Daussant J. beta-Amylases in Cereals : A Study of the Maize beta-Amylase System. Plant Physiol. 1992 Oct;100(2):887-93. doi: 10.1104/pp.100.2.887. PMID: 16653072; PMCID: PMC1075640.
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Amylases in developing barley seeds.

Plant physiology

Bilderback DE.
PMID: 16657792
Plant Physiol. 1971 Sep;48(3):331-4. doi: 10.1104/pp.48.3.331.

The amylases of developing barley seeds (Hordeum vulgare L. cv. Himalaya) were investigated by colorimetric and electrophoretic methods. Maxima of amylolytic activity appeared in the aleurone layers and starchy endosperm at 5 and 20 days after anthesis. Amylase from...

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Bilderback DE. Amylases in developing barley seeds. Plant Physiol. 1971;48(3):331-4doi: 10.1104/pp.48.3.331.
Bilderback, D. E. (1971). Amylases in developing barley seeds. Plant physiology, 48(3), 331-4. https://doi.org/10.1104/pp.48.3.331
Bilderback, D E. "Amylases in developing barley seeds." Plant physiology vol. 48,3 (1971): 331-4. doi: https://doi.org/10.1104/pp.48.3.331
Bilderback DE. Amylases in developing barley seeds. Plant Physiol. 1971 Sep;48(3):331-4. doi: 10.1104/pp.48.3.331. PMID: 16657792; PMCID: PMC396860.
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The genome specific grain proteins and the phylogenetic interrelation between Triticum L., Elytrigia Desf., Elymus L. and Agropyron Gaertn.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Konarev A.
PMID: 24276390
Theor Appl Genet. 1981 Mar;59(2):117-21. doi: 10.1007/BF00285901.

Immunochemical protein studies show that nongliadins of the ethanol-soluble fraction (EF) provide the best biochemical information on genome interrelations in cereals. After electrophoresis (pH 3.2) these genome specific proteins are shown to fall within the category of α-prolamines and...

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Konarev A. The genome specific grain proteins and the phylogenetic interrelation between Triticum L., Elytrigia Desf., Elymus L. and Agropyron Gaertn. Theor Appl Genet. 1981;59(2):117-21doi: 10.1007/BF00285901.
Konarev, A. (1981). The genome specific grain proteins and the phylogenetic interrelation between Triticum L., Elytrigia Desf., Elymus L. and Agropyron Gaertn. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 59(2), 117-21. https://doi.org/10.1007/BF00285901
Konarev, A. "The genome specific grain proteins and the phylogenetic interrelation between Triticum L., Elytrigia Desf., Elymus L. and Agropyron Gaertn." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 59,2 (1981): 117-21. doi: https://doi.org/10.1007/BF00285901
Konarev A. The genome specific grain proteins and the phylogenetic interrelation between Triticum L., Elytrigia Desf., Elymus L. and Agropyron Gaertn. Theor Appl Genet. 1981 Mar;59(2):117-21. doi: 10.1007/BF00285901. PMID: 24276390.
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Genes encoding α-amylase inhibitors are located in the short arms of chromosomes 3B, 3D and 6D of wheat (Triticum aestivum L.).

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Sanchez-Monge R, Barber D, Mendez E, García-Olmedo F, Salcedo G.
PMID: 24247781
Theor Appl Genet. 1986 Apr;72(1):108-13. doi: 10.1007/BF00261464.

Three α-amylase inhibitors, designated Inh. I, II and III have been purified from the 70% ethanol extract of hexaploid wheat (Triticum aestivum L.) and characterized by amino acid analysis, N-terminal amino acid sequencing and enzyme inhibition tests. Inhibitors I...

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Sanchez-Monge R, Barber D, Mendez E, et al. Genes encoding α-amylase inhibitors are located in the short arms of chromosomes 3B, 3D and 6D of wheat (Triticum aestivum L.). Theor Appl Genet. 1986;72(1):108-13doi: 10.1007/BF00261464.
Sanchez-Monge, R., Barber, D., Mendez, E., García-Olmedo, F., & Salcedo, G. (1986). Genes encoding α-amylase inhibitors are located in the short arms of chromosomes 3B, 3D and 6D of wheat (Triticum aestivum L.). TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 72(1), 108-13. https://doi.org/10.1007/BF00261464
Sanchez-Monge, R, et al. "Genes encoding α-amylase inhibitors are located in the short arms of chromosomes 3B, 3D and 6D of wheat (Triticum aestivum L.)." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 72,1 (1986): 108-13. doi: https://doi.org/10.1007/BF00261464
Sanchez-Monge R, Barber D, Mendez E, García-Olmedo F, Salcedo G. Genes encoding α-amylase inhibitors are located in the short arms of chromosomes 3B, 3D and 6D of wheat (Triticum aestivum L.). Theor Appl Genet. 1986 Apr;72(1):108-13. doi: 10.1007/BF00261464. PMID: 24247781.
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Amylolytic microorganism from são paulo zoo composting: isolation, identification, and amylase production.

Enzyme research

Pascon RC, Bergamo RF, Spinelli RX, de Souza ED, Assis DM, Juliano L, Vallim MA.
PMID: 21845217
Enzyme Res. 2011;2011:679624. doi: 10.4061/2011/679624. Epub 2011 Aug 09.

Composting is a way of transforming the organic waste into fertilizer, minimizing the use of inorganic compounds that may contaminate the environment. This transformation is the result of the microorganism action, converting complex carbon sources into energy. Enzymes that...

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Pascon RC, Bergamo RF, Spinelli RX, et al. Amylolytic microorganism from são paulo zoo composting: isolation, identification, and amylase production. Enzyme Res. 2011;2011:679624doi: 10.4061/2011/679624.
Pascon, R. C., Bergamo, R. F., Spinelli, R. X., de Souza, E. D., Assis, D. M., Juliano, L., & Vallim, M. A. (2011). Amylolytic microorganism from são paulo zoo composting: isolation, identification, and amylase production. Enzyme research, 2011679624. https://doi.org/10.4061/2011/679624
Pascon, Renata C, et al. "Amylolytic microorganism from são paulo zoo composting: isolation, identification, and amylase production." Enzyme research vol. 2011 (2011): 679624. doi: https://doi.org/10.4061/2011/679624
Pascon RC, Bergamo RF, Spinelli RX, de Souza ED, Assis DM, Juliano L, Vallim MA. Amylolytic microorganism from são paulo zoo composting: isolation, identification, and amylase production. Enzyme Res. 2011;2011:679624. doi: 10.4061/2011/679624. Epub 2011 Aug 09. PMID: 21845217; PMCID: PMC3154541.
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Biochemical and Thermodynamical Characterization of Glucose Oxidase, Invertase, and Alkaline Phosphatase Secreted by Antarctic Yeasts.

Frontiers in molecular biosciences

Yuivar Y, Barahona S, Alcaíno J, Cifuentes V, Baeza M.
PMID: 29312954
Front Mol Biosci. 2017 Dec 12;4:86. doi: 10.3389/fmolb.2017.00086. eCollection 2017.

The use of enzymes in diverse industries has increased substantially over past decades, creating a well-established and growing global market. Currently, the use of enzymes that work better at ambient or lower temperatures in order to decrease the temperatures...

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Yuivar Y, Barahona S, Alcaíno J, et al. Biochemical and Thermodynamical Characterization of Glucose Oxidase, Invertase, and Alkaline Phosphatase Secreted by Antarctic Yeasts. Front Mol Biosci. 2017;4:86doi: 10.3389/fmolb.2017.00086.
Yuivar, Y., Barahona, S., Alcaíno, J., Cifuentes, V., & Baeza, M. (2017). Biochemical and Thermodynamical Characterization of Glucose Oxidase, Invertase, and Alkaline Phosphatase Secreted by Antarctic Yeasts. Frontiers in molecular biosciences, 486. https://doi.org/10.3389/fmolb.2017.00086
Yuivar, Yassef, et al. "Biochemical and Thermodynamical Characterization of Glucose Oxidase, Invertase, and Alkaline Phosphatase Secreted by Antarctic Yeasts." Frontiers in molecular biosciences vol. 4 (2017): 86. doi: https://doi.org/10.3389/fmolb.2017.00086
Yuivar Y, Barahona S, Alcaíno J, Cifuentes V, Baeza M. Biochemical and Thermodynamical Characterization of Glucose Oxidase, Invertase, and Alkaline Phosphatase Secreted by Antarctic Yeasts. Front Mol Biosci. 2017 Dec 12;4:86. doi: 10.3389/fmolb.2017.00086. eCollection 2017. PMID: 29312954; PMCID: PMC5733001.
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Production of amylases by yeasts.

Canadian journal of microbiology

Linardi VR, Machado KM.
PMID: 22049934
Can J Microbiol. 1990 Nov;36(11):751-3. doi: 10.1139/m90-129.

Yeasts (228) isolated for natural habitats were screened for their ability to produce amylases in semisolid medium of wheat bran. Strains of Aureobasidium pullulans, Candida famata, and Candida kefyr showed high enzymatic activity for α-amylase, glucoamylase, and debranching enzyme....

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Linardi VR, Machado KM. Production of amylases by yeasts. Can J Microbiol. 1990;36(11):751-3doi: 10.1139/m90-129.
Linardi, V. R., & Machado, K. M. (1990). Production of amylases by yeasts. Canadian journal of microbiology, 36(11), 751-3. https://doi.org/10.1139/m90-129
Linardi, V R, and Machado, K M. "Production of amylases by yeasts." Canadian journal of microbiology vol. 36,11 (1990): 751-3. doi: https://doi.org/10.1139/m90-129
Linardi VR, Machado KM. Production of amylases by yeasts. Can J Microbiol. 1990 Nov;36(11):751-3. doi: 10.1139/m90-129. PMID: 22049934.
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Polymorphisms in the α-amy1 gene of wild and cultivated barley revealed by the polymerase chain reaction.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Weining S, Ko L, Henry RJ.
PMID: 24177902
Theor Appl Genet. 1994 Oct;89(4):509-13. doi: 10.1007/BF00225388.

α-Amylases are the key enzymes involved in the hydrolysis of starch in plants. The polymerase chain reaction (PCR) was used to detect polymorphisms in the length of amplified sequences between the annealing sites of two primers derived from published...

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Weining S, Ko L, Henry RJ. Polymorphisms in the α-amy1 gene of wild and cultivated barley revealed by the polymerase chain reaction. Theor Appl Genet. 1994;89(4):509-13doi: 10.1007/BF00225388.
Weining, S., Ko, L., & Henry, R. J. (1994). Polymorphisms in the α-amy1 gene of wild and cultivated barley revealed by the polymerase chain reaction. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 89(4), 509-13. https://doi.org/10.1007/BF00225388
Weining, S, et al. "Polymorphisms in the α-amy1 gene of wild and cultivated barley revealed by the polymerase chain reaction." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 89,4 (1994): 509-13. doi: https://doi.org/10.1007/BF00225388
Weining S, Ko L, Henry RJ. Polymorphisms in the α-amy1 gene of wild and cultivated barley revealed by the polymerase chain reaction. Theor Appl Genet. 1994 Oct;89(4):509-13. doi: 10.1007/BF00225388. PMID: 24177902.
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Showing 13 to 24 of 258 entries