foodsystFood systemsПищевые системы2618-97712618-7272Федеральный научный центр пищевых систем им. В.М. Горбатова РАН10.21323/2618-9771-2023-6-2-188-201foodsyst-269Research ArticleСтатьиEnzyme systems for fragmentation of the rhamnogalacturonan sites main chains in plant tissue protopectin complexФерментные системы для фрагментации основной цепи рамногалактуронановых участков протопектинового комплекса растительной тканиhttps://orcid.org/0000-0002-0913-5644КондратенкоВ. В.KondratenkoV. V.

Кондратенко Владимир Владимирович — кандидат технических наук, доцент, старший научный сотрудник, лаборатория технологии молочнобелковых концентратов, пищевых добавок и производства продуктов на их основе

115093, Москва, ул. Люсиновская, 35/7Тел.: +7–916–328–61–03

Vladimir V. Kondratenko, Candidate of Technical Sciences, Docent, Senior Researcher, Laboratory of Technology for Milk-Protein Concentrates, Food Additives and Products on their Basis

35/7, Lusinovskaya Str., Москва, 115093, RussiaTel.: +7–916–328–61–03

v_kondratenko@vnimi.ruhttps://orcid.org/0000-0001-8237-0774КондратенкоТ. Ю.KondratenkoT. Yu.

Кондратенко Татьяна Юрьевна — старший научный сотрудник, лаборатория технологии пищевых систем общего и специализированного назначения

142703, Россия, Московская область, г. Видное, ул. Школьная, 78Тел.: +7–985–445–76–23

Tatyana Yu. Kondratenko, Senior Researcher, Laboratory of Food Systems Technology for General and Specialized Purposes

78, Shkolnaia Str., 142703, Vidnoe, Moscow region, RussiaTel.: +7–985–445–76–23

t.kondratenko@fncps.ruВсероссийский научно-исследовательский институт молочной промышленностиРоссияRussian Dairy Research InstituteRussian FederationВсероссийский научно-исследовательский институт технологии консервированияРоссияRussian Research Institute of Canning TechnologyRussian Federation20231307202362188201Copyright © Kondratenko V.V., Kondratenko T.Y., 20232023Кондратенко В.В., Кондратенко Т.Ю.Kondratenko V.V., Kondratenko T.Y.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://www.fsjour.com/jour/article/view/269

Special features of the protopectin complex structure of plant tissue suggest the necessity of performing point destruction of certain glycoside bonds in the structure of rhamnogalacturonan polymer chains for industrial production of pectin. These chains include homogalacturonan sites and branching zones. As the homogalacturonan fragments of the protopectin complex carry the main functional load, glycoside bonds between residues of rhamnose and galacturonic acid are targeted bonds. For their directional destruction, it is most expedient to use enzymes of lyase and hydrolase action. The aim of this review is to systemize notions of molecular specific features of enzymes of lyase and hydrolase action that catalyze the process of enzymatic destruction of the rhamnogalacturonan main chain. The paper examines systematics of lyase and hydrolase enzymes by mechanism of destruction of glycoside bonds and by molecular structure. It is shown that the classification data intercross, as a result, each family can include one or several enzyme groups. The review shows the main structural difference of enzymes of lyase and hydrolase action that consists in the obligatory presence of Ca2+ cations in the composition of lyase enzymes. These cations take part in stabilization of conformation of the enzyme molecule and in the catalytic process per se blocking the residue of galacturonic acid. Ca2+ cations are absent in the composition of targeted hydrolase enzymes. Molecular specific features of lyase enzymes determine sensitivity of their catalytic activity to the presence of Ca2+ cations in the system. Exceeding certain concentration can lead to the antagonistic effect. There is no unambiguous idea of this regarding hydrolase enzymes. The review demonstrates the necessity of studying approaches to assessment of expediency of preliminary partial removal of cations from the substrate.

Особенности структуры протопектинового комплекса растительной ткани предполагают необходимость проведения точечной деструкции отдельных гликозидных связей в структуре полимерных цепей рамногалактуронана для промышленного производства пектина. В состав этих цепей входят гомогалактуронановые участки и зоны ветвления. В связи с тем, что основную функциональную нагрузку несут гомогалактуронановые фрагменты протопектинового комплекса, целевыми являются гликозидные связи между остатками рамнозы и галактуроновой кислоты. Для их направленной деструкции наиболее целесообразно использовать ферменты лиазного и гидролазного действия. Целью данного обзора является систематизация представлений о молекулярных особенностях ферментов лиазного и гидролазного действия, катализирующих процесс ферментативной деструкции основной цепи рамногалактуронана. В статье рассматриваются систематики лиазных и гидролазных ферментов по механизму деструкции гликозидных связей и по молекулярной структуре. Показано, что данные классификации пересекаются, в результате чего в каждое семейство может входить как одна, так и несколько групп ферментов. В обзоре показано основное структурное отличие ферментов лиазного и гидролазного действия, заключающееся в обязательном присутствии в составе лиазных ферментов катионов Ca2+. Эти катионы участвуют в стабилизации конформации молекулы фермента и в самом каталитическом процессе, блокируя остаток галактуроновой кислоты. В составе целевых гидролазных ферментов катионы Ca2+ отсутствуют. Молекулярные особенности лиазных ферментов определяют чувствительность их каталитической активности к присутствию катионов Ca2+ в системе. Превышение определенной концентрации способно приводить к антагонистическому эффекту. В отношении гидролазных ферментов однозначное представление на этот счет отсутствует. Показана необходимость исследования подходов к оценке целесообразности предварительного частичного удаления катионов из субстрата.

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The authors declare that there are no conflicts of interest present.