A Comparison of the Action of Several Alpha Amylases upon a Linear Fraction from Corn Starch<sup>1</sup>

Kung, Jo-fen Tung; Hanrahan, Virginia M.; Caldwell, M. L.

doi:10.1021/ja01118a023

Cited by 44 publications

(13 citation statements)

References 9 publications

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“…One can clearly see spectral differences induced by the enzymatic hydrolysis. The action of -amylase upon starch causes hydrolytic cleavages at random -1,4 glucan bonds at the inner part of the starch chains [13], hence the biopolymer starch can not be considered as a homogeneous substrate releasing defined reaction products upon reaction, because it can be hydrolytically cleaved to parts of different chain lengths. Furthermore the substrate itself is altered during the ongoing enzymatic reaction as the fragments remaining after a first hydrolytic cleavage can be accessed again by the enzyme resulting in even smaller molecular weight products.…”

Section: 3mentioning

confidence: 99%

Determination of a-amylase activity using Fourier transform infrared spectroscopy

Krieg¹,

Lendl²,

Vonach³

et al. 1996

Analytical and Bioanalytical Chemistry

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A new method for the determination of alpha-amylase activity in aqueous solutions and human serum with FTIR-spectroscopy is proposed. The chemical reaction catalyzed by the enzyme under study can be followed directly when applying FTIR-spectroscopic detection also in the case, where no colored or electrochemical active species are generated or consumed during the course of the reaction of alpha-amylase with simple starch. Therefore the determination of the alpha-amylase activity could successfully be performed by recording two FTIR-spectra, one immediately after mixing the sample and a substrate (starch-) solution and the other after a 20 min reaction time. From these two FTIR-spectra a difference spectrum was calculated hereby eliminating an unspecific absorption of the matrix. The intensities of the resulting difference spectra corresponded to the extent of the reaction which took place during the investigated time interval and hence could be related to the activity of the enzyme in the sample. The developed method is linear from 80 to 1400 U/l (r.s.d.=5% for 700 U/l) in aqueous solutions and was also successfully applied to the determination of alpha-amylase activity in human serum where a linear working range from 100 to 800 U/l (r.s.d.=11% for 150 U/l) was achieved.

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Section: 3mentioning

confidence: 99%

Determination of a-amylase activity using Fourier transform infrared spectroscopy

Krieg¹,

Lendl²,

Vonach³

et al. 1996

Analytical and Bioanalytical Chemistry

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“…Gluconamylase는 starch에 작용하여 amylose와 amylopectin의 α-1,4, α-1,6 결합을 가수분해하여 glucose를 생성하 는 당화효소이며, isoamylase는 starch의 α-1,6 결합에만 작용 하는 효소이다 [3,4,9]. 이러한 전분의 분해에 관련하는 효소는 효모, 곰팡이, 세균, 맥아 및 동물체내에 널리 존재한다.…”

Section: 서 론unclassified

Amylase Activity and Characterization of Microorganism Isolated from in Aquacultural Effluents Sediment Layer

Kim¹,

Jang²,

Harikrishnan³

et al. 2009

Journal of Life Science

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-In the course of screening of useful enzyme-producing microorganisms from marine sedimentary layers, we isolated 2 amylase producing strains and tested their amylase producing activities. Analyses of 16S rDNA sequences and biochemical methods (BIOLOG) of two isolates showed that they were confirmed to be a gram positive Bacillus sp. and gram negative Pseudoalteromonas sp., respectively. Excellent amylase producing strains were termed Bacillus sp. and Pseudoalteromonas sp. ST-140, and further studies were conducted on their amylase producing characteristics. Optimum conditions for cell growth in amylase activity were obtained when the isolate (Bacillus sp. ST-63 and Pseudoalteromonas sp. ST-140) was cultured at 30 o C and pH 7～8.

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“…68 ences in action patterns, distinguishes between a-and {3-amylases, and is independent of enzyme concentration. The method of Kung, Hanrahan, and Caldwell (1953) was employed utilizing amylose and amylopectin as substrates.…”

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confidence: 99%

A Comparison of Alpha‐amylases From the Latex of Three Selected Species of Euphorbia (Euphorbiaceae)

Biesboer

Mahlberg

1981

American J of Botany

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A technique for the partial purification of α‐amylases from latex of Euphorbia heterophylla, E. marginata, and E. tirucalli is described. The enzymes were found to be similar to other higher plant amylases using the criteria of molecular weight, pH characteristics, kinetics, number of isozymes, and blue value‐reducing value patterns. Carbohydrases other than α‐amylases were not detectable in latex. The amylases were employed to examine their capacity to digest latex starch grains which are common components of the laticiferous cell in this genus. Laticifer starch grains are not susceptible to in vitro amylolysis. Removal of the starch grain membrane with Triton X‐100, damaging the grain, or treating the grains with α‐amylases from diverse biological sources had little effect upon hydrolysis. Grains incubated with pullulanase followed by α‐amylase caused a slight but significant increase in hydrolysis of raw laticifer starch grains. These studies indicate that the nonarticulated laticifer in Euphorbia is a cul de sac for certain primary and secondary metabolic products and that the indigestible and morphologically complex starch grains in the latex have evolved to function in a secondary role within the laticifer.

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A Comparison of the Action of Several Alpha Amylases upon a Linear Fraction from Corn Starch¹

Cited by 44 publications

References 9 publications

Determination of a-amylase activity using Fourier transform infrared spectroscopy

Determination of a-amylase activity using Fourier transform infrared spectroscopy

Amylase Activity and Characterization of Microorganism Isolated from in Aquacultural Effluents Sediment Layer

A Comparison of Alpha‐amylases From the Latex of Three Selected Species of Euphorbia (Euphorbiaceae)

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A Comparison of the Action of Several Alpha Amylases upon a Linear Fraction from Corn Starch1

Cited by 44 publications

References 9 publications

Determination of a-amylase activity using Fourier transform infrared spectroscopy

Determination of a-amylase activity using Fourier transform infrared spectroscopy

Amylase Activity and Characterization of Microorganism Isolated from in Aquacultural Effluents Sediment Layer

A Comparison of Alpha‐amylases From the Latex of Three Selected Species of Euphorbia (Euphorbiaceae)

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A Comparison of the Action of Several Alpha Amylases upon a Linear Fraction from Corn Starch¹