Production and biochemical characterization of halotolerant β-glucosidase by Penicillium roqueforti ATCC 10110 grown in forage palm under solid-state fermentation

• Published in: Biomass conversion and biorefinery Vol. 12; no. 8; pp. 3133 - 3144
• Main Authors: das Neves, Cíntia Albernaz, de Menezes, Luiz Henrique Sales, Soares, Glêydison Amarante, dos Santos Reis, Nadabe, Tavares, Iasnaia Maria Carvalho, Franco, Marcelo, de Oliveira, Julieta Rangel
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01-08-2022; Springer Nature B.V
• Subjects: Biotechnology; Calcium ions; Cobalt; Dichloromethane; Energy; Ethanol; Ethylenediaminetetraacetic acids; Fermentation; Fungi; Glucosidase; Industrial applications; Lactose; Moisture content; Moisture effects; Optimization; Original Article; Renewable and Green Energy; Solid state; Statistical models; Substrates; Prickly pear; Biochemical characterization; Central composite rotational design; Cellulases
• ISSN: 2190-6815; 2190-6823
• DOI: 10.1007/s13399-020-00930-8

This study investigated for the first time the production of
β
-glucosidase from
Penicillium roqueforti
ATCC 10110 by solid-state fermentation using the forage palm (
Nopalea cochenillifera
) as a substrate. For the optimization of incubation parameters, time, and temperature, the central composite rotational statistical model was used, resulting in an increase in enzymatic activity, by 94.70% with a maximum yield of 935.07 ± 21.70 IU/g at 23 °C and 56% moisture content. The
β
-glucosidase produced to show higher reactivity and stability at pH 5.0 at 52 °C. In addition to good halotolerance, maintaining 139.93% and 95.34% of the residual activity in the reaction and 57.93% and 94.28% after 24 h of incubation. The addition of Na
+
, Fe
2 +
, Mg
2+
, EDTA, Triton X-100, lactose, and dichloromethane improved
β
-glucosidase activity, while Ca
2+
, Zn
2+
, and Co
2+
were not expressed, and SDS, ethanol, acetone, and methanol were inhibitors. Therefore, it was possible to produce
β
-glucosidase with a halotolerant profile, indicating a promising alternative to obtain this enzyme for biotechnological and industrial applications.