Диссертация (1152193), страница 18
Текст из файла (страница 18)
– 482 с.13. Номенклатураферментов:РекомендацииМеждународногобиохимического союза по номенклатуре и классификации ферментов,символам кинетики ферментативных реакций / перевод с англ. под ред.А.Е. Браунштейна. – М.: ВИНИТИ, 1979. – 322 с.14. Rawlings N.D. The MEROPS database of proteolytic enzymes, their substratesand inhibitors in 2017 and a comparison with peptidases in the PANTHERdatabase / N.D. Rawlings, A.J.
Barrett, P.D. Thomas, X. Huang, A. Bateman,R.D. Finn // Nucleic Acids Res. – 2018. – V. 46. – P. 624–632.15. ЛаврентьеваЕ.В.Основымолекулярныхмеханизмоврегуляцииэкспрессии генов пептидаз в прокариотной клетке / Е.В. Лаврентьева, Т.Г.Банзаракцаева, А.А. Раднагуруева, Л.Б. Буянтуева / Под ред. Б.Б.Намсараева. – Улан-Удэ, 2012. – 66 с12216. Ежова Г.П. Биоинформационные аспекты протеомики и деградации белка/ Г.П.
Ежова, А.А. Бабаев, В.В. Новиков. – Нижний Новгород, 2007. – 86c.17. Gonzales T. Bacterial amino peptidase: properties and functions / T. Gonzales,J. Robert-Baudouy // FEMS Microbiol Rev. – 1996. – V. 18. – P. 319–344.18. Strater N. Leucyl aminopeptidase (animal and plant) // Handbook of ProteolyticEnzymes / N. Strater, W.N. Lipscomb / Ed. A. Barret, N.D. Rawlings, J.F.Woessner.
– NY: Academic press., 1998. – ch. 473. – P. 1384–1389.19. Lazdunski A. Peptidases and proteases of Escherichia coli and Salmonellatyphimurium / A. Lazdunski // FEMS Microbiol Rev. – 1989. – V. 63. – P.265–276.20. Rawlings N.D. Introduction: metallopeptidases and their clans // Handbook ofProteolytic Enzymes / N.D. Rawlings, A.J. Barrett; edited by J.F. Woesner. –Second edition. – USA: Elsevier/Academic Press, 2004. – P. 231–263.21. Rahulan R. Characterization of leucine amino peptidase from Streptomycesgedanensis and its applications for protein hydrolysis / R.
Rahulan, K.S. Dhar,K.M. Nampoothiri, A. Pandey // Process Biochemistry. – 2012. – V. 47. – P.234–242.22. Adams M.W.W. Enzymes and proteins from organisms that grow near andabove 100℃ / M.W.W. Adams // Annu Rev Microbiol. – 1993. – V. 47. – P.627–658.23. Nampoothiri K.M. L-leucine aminopeptidase production by filamentousAspergillus fungi / K.M. Nampoothiri, V. Nagy, K. Kovacs, G. Szakacs, A.Pandey // Letters in Applied Microbiology. – 2005. – V.
41. – P. 498–504.24. Clemente A. Enzymatic protein hydrolysates in human nutrition / A. Clemente// Trends Food Sci Technol. – 2000. – V. 11. – P. 254–262.25. Toldra F. Contribution of muscle amino peptidase to flavor development in drycured ham / F. Toldra, A.C. Aristoy, M. Flores // Food Res. – 2000.
– Int. 33. –P. 181–185.12326. Gobbetti M. The proteolytic system of Lactobacillus sanfrancisco CB1:purification and characterization of a proteinase, a dipeptidase, and anaminopeptidase / M. Gobbetti, E. Smacchi, A. Corsetti // Appl. Environ.Microbiol. – 1996. – V. 62. – P. 3220-3226.27. Shie-Jea L. Extracellular leucine aminopeptidase produced by Aspergillusoryzae LL1 and LL2 / L. Shie-Jea, Ch.
Li-Lin, W. Chiou-Yen, Ch. Wen-Shen //African Journal of Microbiology Research. – 2010. – V. 4(3). – P. 158-168.28. Грачева И.М. Технология ферментных препаратов / И.М. Грачева, А.Ю.Кривова. – 3-е изд., перераб. и доп. – М.: Элевар, 2000. – 512 с.29.
Laskar A. Modeling and structural analysis of evolutionarily diverse S8 familyserine proteases / A. Laskar, E.J. Rodger, A. Chatterjee, C. Mandal //Bioinformation. – 2011. – V. 7(5). – P. 239-245.30. Hedstrom L. Serine protease mechanism and specificity / L. Hedstrom // Chem.Rev. – 2002. – V. 102. – P. 4501-4523.31. Page M.J. Serine peptidases: Classification, structure and function / M.J. Page,E. Di Cera // Cell. Mol. Life Sci.
– 2008. – V.65. – P. 1220 – 1236.32. Polgár L. The catalytic triad of serine peptidases / L. Polgár // CMLS. – 2005. –V. 62. – P. 2161–2172.33. Tripathi L.P. Genome-wide survey of prokaryotic serine proteases: Analysis ofdistribution and domain architectures of five serine protease families inprokaryotes / L.P. Tripathi, R.
Sowdhamini // BMC Genomics. – 2008. – V. 9.– P. 549-576.34. Немова Н.Н. К вопросу об эволюции протеолитических ферментов / Н.Н.Немова, Л.А. Бондарева // Биомедицинская химия. – 2008. – Т. 54(1). – С.42-57.35. Czapinska R. Structural and energetic determinants of the S1-site specifity inserine proteases / R. Czapinska, J. Otlenski // Eur. J. Bioch. – 1999. – V.260. –P. 571-595.36. Руденская Г.Н.
Новые подсемейства субтилизинов / Г.Н. Руденская //Биоорг. Химия. – 1994. – B. 20(5). – С. 475–484.12437. Bedford M.R. Enzymes in farm animal nutrition / M.R. Bedford, G.G.Partridge. – UK: CAB International, 2010. – 319 p.38. Tremacoldi C.R. Purification and properties of an alkaline protease ofAspergillus clavatus / C.R. Tremacoldi, R. Monti, H.S. Selistre-De-Araujo,E.C.
Carmona // World J. Microbiol. Biotechnol. – 2007. – V. 23. – P. 295–299.39. Barett A.J. Handbook of Proteolytic Enzymes / A.J. Barett, N.D. Rawlings, J.F.Woessner (Eds). – 3rd Edition. – San Diego: Academic Press, 2012. – 4104 p.40. Kudryavtseva O.A. Fungal proteolytic enzymes: features of the extracellularproteases of xylotrophic basidiomycetes / O.A. Kudryavtseva, Ya.E.Dunaevsky, O.V. Kamzolkina, M.A.
Belozersky // Mikrobiologiya. – 2008. –V. 77(6). – P. 725–73741. Barett A.J. Proteolytic enzymes: aspartic and metallopeptidases / A.J. Barett //Methods Enzymol. – 1995. – V. 248. – P. 183.42. Palashoff M.H. Determining the specificity of pepsin for proteolytic digestion:Chemistry Master's Theses / Palashoff Melissa H. – Northeastern UniversityBoston, Massachusetts, 2008. – 144 p.43. Sielecki A.R. Refined structure of porcine pepsinogen at 1,8A resolution / A.R.Sielecki, M. Fujinaga, R.J.
Read, N.G. James // J. Mol. Biol. – 1991. – V. 219.– P. 671–692.44. Polgar L. The mechanism of action of aspartic proteases involves 'push-pull'catalysis / L. Polgar // Federation of European Biochemical Societies. – 1987. –V. 219(1). – P. 1–4.45. Davies D.R. The structure and function of the aspartic proteinases / D.R.Davies // Annu. Rev. Biophys.
Biophys. Chern. – 1990. – V. 19. – P. 189-215.46. Sielecki A.R. Molecular and crystal structures of monoclinic porcine pepsinrefined at 1.8 A resolution / A.R. Sielecki, A.A. Fedorov, et al. // J. Mol. Biol. –1990. – V. 214. – P. 143-170.47. Dunn B.M. Overview of pepsin-like aspartic peptidases / B.M.
Dunn // Curr.Protoc. Protein Sci. – 2001. – Ch. 21. – P. 21-23.12548. James M.N. Molecular structure of an aspartic proteinase zymogen, porcinepepsinogen, at 1.8 A resolution / M.N. James, A.R. Sielecki // Nature. – 1986. –V. 319 (6048). – P. 33-38.49. Fruton J.S. The specificity and mechanism of pepsin action / J.S. Fruton //Enzymol. Relat. Areas. Mol. Biol. – 1970. – V. 33. – P. 401-443.50. Zhang Z. Determination of amide hydrogen exchange by mass spectrometry: anew tool for protein structure elucidation / Z.
Zhang, D.L. Smith // Protein Sci.– 1993. – V. 2. – P. 522-531.51. Пащенко Л.П. Функциональные пищевые продукты на основе пищевойкомбинаторики / Л.П. Пащенко, Е.Е. Курчаева, М.П. Бахмет // Известиявузов. Пищевая технология. – 2012. – № 2–3. – C. 84–87.52.
Телишевская Л.Я. Белковые гидролизаты. Получение, состав, применение/ Л.Я Телишевская. – М.: Аграрная наука, 2000. – 295 с.53. СмагинаА.В.Анализиспользованиясоевогобелкавпищевойпромышленности / А.В. Смагина, М.В. Сытова // Научные трудыДальрыбвтуза. – 2011.
– № 23. – C. 73-78.54. Долгополова Н.В. Значение озимой и яровой пшеницы в производствепродуктов питания / Н.В. Долгополова, В.А. Скрипин, О.М. Шершнёва,Ю.В.Алябьева//ВестникКурскойгосударственнойсельскохозяйственной академии. – 2009. – № 5. – С. 52–56.55. Казаков Е.Д. Биохимия зерна и хлебопродуктов / Е.Д. Казаков, Г.П.Карпиленко. – 3-е изд., перераб. и доп.
– СПб.: ГИОРД, 2005. – 512 с.56. Šramkováa Z. Chemical composition and nutritional quality of wheat grain / Z.Šramkováa, E. Gregováb, E. Šturdíka // Acta Chimica Slovaca. – 2009. – V.2(1). – P. 115-138.57. Koehler P. Chemistry of Cereal Grains // Handbook on SourdoughBiotechnology / P.
Koehler, H. Wieser / Ed. M. Gobbetti, M. Ganzle. – NY:Springer Science+Business Media, 2013. – Ch.2. – P. 11-45.12658. Нечаев А.П. Пищевая химия / А.П. Нечаев, С.Е. Траубенберг, А.А.Кочеткова и др.; Под ред. А.П. Нечаева. – 4-е изд., испр. и доп. – СПб:ГИОРД, 2007. – 640 с.59. Kowieska A. Chemical composition and nutritional characteristics of severalcereal grain / A. Kowieska, R. Lubowicki, I. Jaskowska // Acta Sci. Pol.,Zootechnica. – 2011.
– V. 10 (2). – P. 37–50.60. Кислухина О.В. Биотехнологические основы переработки растительногосырья / О.В. Кислухина, И.И. Кюдулас. – Каунас: Технология, 1997. – 183с.61. Stone B.A Chemistry and biology of 1,3-β-glucans / B.A. Stone, A.E. Clarke. –Bundoora: La Trobe University Press, 1992. – 803 p.62. Растительный белок / Пер.
с фр. В.Г. Долгополова; Под ред. Т.П.Микулович. – М.: Агропромиздат, 1991. – 684 с.63. Geisenhoff H. Bitterness of soy protein hydrolysates according to molecularweight of peptides: Graduate Theses and Dissertations Master of Science /Geisenhoff Heidi. – Iowa State University, Iowa, 2009. – 107 p.64. Gibbs B.F. Production and characterization of bioactive peptides from soyhydrolysate and soy-fermented food / B.F. Gibbs, A. Zougman, R. Masse, C.Mulligan // Food Research International.
– 2004. – V.37. – P. 123–131.65. Peisker M. Manufacturing of soy protein concentrate for animal nutrition / M.Peisker // Cahiers Options Mediterraneennes. – 2001. – V. 54. – P. 103-107.66. Yang W.W. Soybean allergens: presence, detection and methods for mitigation,soybean and health / W.W. Yang, E. Gonzalez de Mejia, H. Zheng, Y. Lee;Edited by Prof. Hany El-Shemy. – InTech, 2011.
![](https://s.studizba.com/z.php?f=/templates/si/i/noavatar.png&w=100&h=100&t=1"){kind=avatar}
