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Physico-chemical properties and substrate specificity of α-(1→3)-D-glucan degrading recombinant mutanase from Trichoderma harzianum expressed in Penicillium verruculosumстатья Исследовательская статья
- Авторы: Sinitsyna O.A., Volkov P.V., Zorov I.N., Rozhkova A.M., Emshanov O.V., Romanova Y.M., Komarova B.S., Novikova N.S., Nifantiev N.E., Sinitsyn A.P.
- Журнал: Applied and Environmental Microbiology
- Год издания: 2025
- Издательство: American Society for Microbiology
- Местоположение издательства: United States
- Номер статьи: e0022624
- DOI: 10.1128/aem.00226-24
- Аннотация: The gene mutAW encoding Trichoderma harzianum fungus mutanase (MutA, GH71 family, α-1,3-glucanase, EC 3.2.1.59) was cloned and heterologously expressed by the highly productive Penicillium verruculosum fungus. P. verruculosum MutA strain secreted crude enzyme preparations with the recombinant MutA content of 40% of the total secreted protein, and the specific activity increased 150 folds compared to that of enzyme preparation obtained by the host strain. Homogeneous MutA had molecular mass of 70 kDa and displayed maximum of the activity on mutan at pH 5.0 and 50°C, with Km and kcat being 1.0 g/L and 30 s-1, respectively. At 40-50°C, the MutA was stable for at least 3 h. Glucose was the main product of long-term mutan hydrolysis. HPLC analysis of hydrolysis product of oligo-α-(1→3)-D-glucosides bearing UV-detectable N-trans-cinnamoyl residue in the aglycon clearly indicated that MutA has an endo-processive hydrolytic mode of action. It was demonstrated that MutA can destroy the polysaccharide matrix of both gram-positive and gram-negative pathogenic bacteria biofilms.
- Добавил в систему: Синицын Аркадий Пантелеймонович
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Экспертное_заключение_1.pdf | Экспертное_заключение_1.pdf | 286,0 КБ | 17 февраля 2025 [aps306cellulas] | |
| 2. | Полный текст | 25_aim_a-glucan.pdf | 1,9 МБ | 17 февраля 2025 [aps306cellulas] |