Oxidation of amino acids by peroxomonophosphoric acid?a kinetic study

ABSTRACT A new starch-binding domain (SBD) was recently described in α-amylases from three lactobacilli (Lactobacillus amylovorus, Lactobacillus plantarum, and Lactobacillus manihotivorans). Usually, the SBD is formed by 100 amino acids, but the SBD sequences of the mentioned lactobacillus α-amylases consist of almost 500 amino acids that are organized in tandem repeats. The three lactobacillus amylase genes share more than 98% sequence identity. In spite of this identity, the SBD structures seem to be quite different. To investigate whether the observed differences in the SBDs have an effect on the hydrolytic capability of the enzymes, a kinetic study of L. amylovorus and L. plantarum amylases was developed, with both enzymes acting on several starch sources in granular and gelatinized forms. Results showed that the amylolytic capacities of these enzymes are quite different; the L. amylovorus α-amylase is, on average, 10 times more efficient than the L. plantarum enzyme in hydrolyzing all the tested polymeric starches, with only a minor difference in the adsorption capacities.

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Kinetic Study of Apo B100 Containing Lipoprotein Metabolism Using Amino Acids Labeled with Stable Isotopes: Methodological Aspects

Clinical Chemistry and Laboratory Medicine (CCLM) ◽

10.1515/cclm.1998.131 ◽

1998 ◽

Vol 36 (10) ◽

Cited By ~ 6

Author(s):

Cyrille Maugeais ◽

Khadija Ouguerram ◽

Michel Krempf ◽

Thierry Magot

Keyword(s):

Amino Acids ◽

Stable Isotopes ◽

Kinetic Study ◽

Lipoprotein Metabolism ◽

Methodological Aspects

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MECHANISTIC INVESTIGATION OF OXIDATION OF SOME AMINO ACIDS BY BIS(DIHYDROGEN TELLURATE)ARGENTATE(III) ION IN ALKALINE MEDIUM: A KINETIC STUDY

Journal of the Chilean Chemical Society ◽

10.4067/s0717-97072009000400013 ◽

2009 ◽

Vol 54 (4) ◽

Author(s):

SHUYING HUO ◽

CHANGYING SONG ◽

JINHUAN SHAN ◽

SHIGANG SHEN ◽

HANWEN SUN

Keyword(s):

Amino Acids ◽

Kinetic Study ◽

Alkaline Medium ◽

Mechanistic Investigation

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Oxidative Decarboxylation and Deamination of Essential Amino Acids by Nicotinium Dichromate - A Kinetic Study

International Letters of Chemistry Physics and Astronomy ◽

10.18052/www.scipress.com/ilcpa.45.66 ◽

2015 ◽

Vol 45 ◽

pp. 66-72

Author(s):

K. Vivekanandan ◽

R. Lakshmi Narayanan

Keyword(s):

Amino Acids ◽

Ionic Strength ◽

Kinetic Study ◽

Aqueous Medium ◽

Perchloric Acid ◽

Sodium Perchlorate ◽

Essential Amino Acids ◽

Oxidative Decarboxylation ◽

First Order ◽

Different Temperatures

The oxidation of essential amino acids like valine, leucine, isoleucine, threonine, phenylalanine and histidine using nicotinium dichromate in aqueous medium in presence of perchloric acid at 313 K leads to the formation of corresponding aldehydes. The reaction is first order with respect to nicotinium dichromate, fractional order with respect to amino acids and second order with respect to perchloric acid. Increase in ionic strength by the addition of sodium perchlorate has no effect on the rate constant. There is no polymerization with acrylonitrile. The reaction has been studied at different temperatures and a mechanism confirming to the kinetic observations is suggested.

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