Lignocellulolytic enzyme activity pattern of three white oyster mushroom (Pleurotus ostreatus (Jacq.) P. Kumm.) strains during mycelial growth and fruiting body development
| العنوان: | Lignocellulolytic enzyme activity pattern of three white oyster mushroom (Pleurotus ostreatus (Jacq.) P. Kumm.) strains during mycelial growth and fruiting body development |
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| المؤلفون: | N Nurfitri, I Saskiawan, W Mangunwardoyo |
| المصدر: | Journal of Physics: Conference Series. 1725:012056 |
| بيانات النشر: | IOP Publishing, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | History, Mushroom, Oyster, biology, Chemistry, biology.organism_classification, Enzyme assay, Computer Science Applications, Education, White (mutation), Horticulture, biology.animal, biology.protein, Pleurotus ostreatus, Mycelium |
| الوصف: | Pleurotus ostreatus is one of the edible mushrooms that can utilize lignocellulose as substrate because of their ability to secrete the lignocellulolytic enzyme. The purpose of this research is to investigate and compare the lignocellulolytic enzymes production of P. ostreatus InaCC F209, F216 and LIPI on solid-state fermentation using sawdust during 70 days of mycelial growth (vegetative phase) and fruiting body development (reproductive phase). Supernatant of the extracted enzyme solutions were employed to investigate the reducing sugar, soluble protein, and enzyme activities. The results revealed that reducing sugar concentration of the three P. ostreatus strains subjected increased during growth and reached the maximum concentration on the reproductive phase, while the total protein content fluctuated during the growth but reached the maximum concentration on the reproductive phase. Laccase, LiP, and MnP activities of three P. ostreatus strains were higher on the vegetative phase, while the endoxylanase and endoglucanase activities were higher on the reproductive phase. β-glucosidase activity showed different variations between three P. ostreatus strains. Pleurotus ostreatus InaCC F209 produced the highest and most stable laccase, β-glucosidase, endoglucanase, and endoxylanase than two others. |
| تدمد: | 1742-6596 1742-6588 |
| DOI: | 10.1088/1742-6596/1725/1/012056 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_________::078637cb90aa3d8219648e3aa3fc871d https://doi.org/10.1088/1742-6596/1725/1/012056 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi...........078637cb90aa3d8219648e3aa3fc871d |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 17426596 17426588 |
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| DOI: | 10.1088/1742-6596/1725/1/012056 |