4.6 Article

Comparison of Trichoderma longibrachiatum Xyloglucanase Production Using Tamarind (Tamarindus indica) and Jatoba (Hymenaea courbaril) Seeds: Factorial Design and Immobilization on Ionic Supports

期刊

FERMENTATION-BASEL
卷 8, 期 10, 页码 -

出版社

MDPI
DOI: 10.3390/fermentation8100510

关键词

xyloglucanase; Trichoderma longibrachiatum; Hymenaea courbaril; Tamarindus indica; enzyme immobilization

资金

  1. Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2017/25862-6, 2021/070663, 2017/23989-9, 2017/09000-4]
  2. National Institute of Science and Technology of Bioethanol [FAPESP 2014/50884-5]
  3. FAPESP-FCT-Fundacao para a Ciencia e Tecnologia de Portugal [2018/07522-6]
  4. Conselho Nacional de Desenvolvimento Cientifico (CNPq) [465319/2014-9, 310340/2021-7]
  5. Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES) [001]

向作者/读者索取更多资源

This study optimized the production of xyloglucanase from Trichoderma longibrachiatum using tamarind and jatoba seeds as carbon sources, and successfully immobilized the enzyme on ionic supports. The study found that tamarind seeds had higher activity than jatoba seeds, and scaling up the production increased the enzyme activity.
Xyloglucan (XG) is the predominant hemicellulose in the primary cell wall of superior plants. It has a fundamental role in controlling the stretching and expansion of the plant cell wall. There are five types of enzymes known to cleave the linear chain of xyloglucan, and the most well-known is xyloglucanase (XEG). The immobilization process can be used to solve problems related to stability, besides the economic benefits brought by the possibility of its repeated use and recovery. Therefore, this study aims at the optimization of the xyloglucanase production of Trichoderma longibrachiatum using a central composite rotatable design (CCRD) with tamarind and jatoba seeds as carbon sources, as well as XEG immobilization on ionic supports, such as MANAE (monoamine-N-aminoethyl), DEAE (diethylaminoethyl)-cellulose, CM (carboxymethyl)-cellulose, and PEI (polyethyleneimine). High concentrations of carbon sources (1.705%), at a temperature of 30 degrees C and under agitation for 72 h, were the most favorable conditions for the XEG activity from T. longibrachiatum with respect to both carbon sources. However, the tamarind seeds showed 23.5% higher activity compared to the jatoba seeds. Therefore, this carbon source was chosen to continue the experiments. The scaling up from Erlenmeyer flasks to the bioreactor increased the XEG activity 1.27-fold (1.040 +/- 0.088 U/mL). Regarding the biochemical characterization of the crude extract, the optimal temperature range was 50-55 degrees C, and the optimal pH was 5.0. Regarding the stabilities with respect to pH and temperature, XEG was not stable for prolonged periods, which was crucial to immobilizing it on ionic resins. XEG showed the best immobilization efficiency on CM-cellulose and DEAE-cellulose, with activities of 1.16 and 0.89 U/g of the derivative (enzyme plus support), respectively. This study describes, for the first time in the literature, the immobilization of a fungal xyloglucanase using these supports.

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