Информация о статье

Количество просмотров: 2135

Название статьи Screening and Identification of Pigmental Yeast Producing L-phenylalanine Ammonia-Lyase and Their Physiological and Biochemical Characteristics
Авторы

Babich O., Kemerovo Institute of Food Science and Technology, The Russian Federation, Kemerovo, olich.43@mail.ru

Раздел: BIOTECHNOLOGY
Год 2014 Номер журнала 2 DOI 579.67
Аннотация The results of the analysis of DNA sequences encoding L-phenylalanine ammonia-lyase (PAL) synthesis, performed to obtain universal primers complementary to conserved regions of the pal gene, are presented in the article. The fragment of pal gene was amplified in organisms under study. Nucleotide sequence of the pal gene in microorganisms exhibiting L-phenylalanine ammonia-lyase activity was determined by DNA sequencing. The results of its comparison with the corresponding sequences of known species are presented. Phenotypic characteristics and biochemical properties of selected cultures were studied. An investigation aimed to choose a superproducer strain of L-phenylalanine ammonia-lyase was conducted. It was found that L-phenylalanine ammonia-lyase synthesis was the most active in the following strains: Aureobasidium pullulans Y863, Rhodosporidium infirmominiatum Y1569, Candida glabrata Y2813, Candida maltose Y242, Debaryomyces robertsiae Y3392, Rhodosporidium diobovatum Y1565, Rhodotorula lactose Y2770, Saccharomyces cerevisiae Y1127, Tilletiopsis washingtonensis Y1650, Torulopsis apicola Y566, Tremella foliacea Y1624, Rhodotorula rubra Y1193, and Debaryomyces castellii Y968. This allows recommending them for further research aimed to obtain the enzyme preparation of L-phenylalanine ammonia-lyase.
Ключевые слова L-phenylalanine ammonia-lyase, enzyme, pal gene, pigmental yeast, nucleotide sequence, amino acid sequence, phylogenetic tree
Информация о статье Дата поступления 30 ноября -0001 года
Дата принятия в печать 30 ноября -0001 года
Дата онлайн-размещения 30 ноября -0001 года
Выходные данные статьи Babich O. Screening and Identification of Pigmental Yeast Producing L-phenylalanine Ammonia-Lyase and Their Physiological and Biochemical Characteristics / Babich O. // Food and Raw Materials. - 2014. - no. 2. - P. 75-87
Загрузить полный текст статьи
Список цитируемой литературы
  1. Sarkissian, C.N., and Gamez, A., Phenylalanine ammonia lyase, enzyme substitution therapy for phenylketonuria, where are we now? Mol. Genet. Metab., 2005. vol. 86, P. 22-26.
  2. Rother, D., Poppe, L., Morlock, G., Viergutz, S., and Re'tey, J., An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum, Eur. J. Biochem., 2002. vol. 269, P. 3065-3075.
  3. Dixon, R.A., Stress-induced phenylpropanoid metabolism, Plant Cell, 1995. vol. 7, P. 1085-1097.
  4. Bezanson, G.S., Desaty, D., Emes, A.V., and Vining, L.C., Biosynthesis of cinnamamide and detection of phenylalanine ammonia-lyase in Streptomyces verticillatus, Can. J. Microbiol., 1970. vol. 16, P. 147-151.
  5. Gilbert, H.J., The effect of proteinases on phenylalanine ammonia-lyase from the yeast Rhodotorula glutinis, Biochem., 1981. vol. 199, P. 715-723.
  6. Evans, C.T., Hanna, K., Payne, C., Conrad, D., and Misawa, M., Biotransformation of trans-cinnamic acid to L-phenylalanine: Optimization of reaction conditions using whole yeast cells, Enzyme Microb. Technol., 1987. vol. 9, P. 417-421.
  7. Hodgins, C.W., and Stith, D.S., An in vivo evaluation of the chemotherapeutic potency of phenylilalanine ammonia-lyase, Cancer Research, 1973. vol. 33, P. 2529-2532.
  8. Sarkissian, C.N., Shao, Z., Blain, F., Peevers, R., Su, H., Heft, R., Chang, T.M.S., and Scriver, C.R., A different approach to treatment of phenylketonuria: Phenylalanine degradation with recombinant phenylalanine ammonia lyase, Proc. Natl. Acad. Sci. USA, 1999. vol. 96, P. 2339-2344.
  9. Leyva, A., Liang, X., Pintor-Toro, J.A., and Dixon, R.A., Ciselement combinations determine phenylalanine ammonia-lyase gene tissue-specific expression patterns, Plant Cell, 1992. vol. 4, P. 263-271.
  10. Church, G.M., and Gilbert, W., Genomic Sequencing, Proc. Natl. Acad. Sci. USA, 1991. vol. 22, P. 1991-1995.
  11. Cochrane, F.C., Davin, L.B., and Lewis, N.G., The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms, Phytochemistry, 2004. vol. 65, P. 1557-1564.
  12. Dixon, R.A., and Brown, M., Ward Modulation of L-phenylalanine ammonia-lyase by pathway intermediates in cell suspension cultures of dwarf French bean (Prtaseo/us vulgaris L), Planta, 1980. vol. 150, P. 279-285.
  13. Genosistematika - chto eto takoe? (Genosystematics: What is it?) http://www.rusbiotech.ru/article/.
  14. Babich, O.O., Prosekov, A.Yu., and Soldatova, L.S., Modeling of a continuous biotechnological process of L-phenylalanine ammonia-lyase production, Izvestiya vysshykh uchebnykh zavedenii. Seriya: Khimiya i khimicheskie tekhnologii (Higher Education Institution Herald. Chemistry and chemical technology series), 2013. vol. 56 (4), P. 106-109.

Copyright © 2014, KemIFST. This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), allowing third parties to copy and redistribute the material in any medium or format and to remix, transform, and build upon the material for any purpose, even commercially, provided the original work is properly cited and statesitslicense. This article is published with open access at http://frm-kemtipp.ru.