4.7 Article

Production, immobilization and characterization of beta-glucosidase for application in cellulose degradation from a novel Aspergillus versicolor

期刊

出版社

ELSEVIER
DOI: 10.1016/j.ijbiomac.2021.02.154

关键词

Beta-glucosidase; Aspergillus versicolor; Immobilization

资金

  1. National Natural Science Foundation of China [82073963, 81522049]
  2. Zhejiang Provincial Ten Thousand Program for Leading Talents of Science and Technology Innovation [2018R52050]
  3. Zhejiang Provincial Program for the Cultivation of High-Level Innovative Health Talents
  4. Zhejiang Provincial Natural Science Foundation of China [LQ20C010004]
  5. Zhejiang Chinese Medical University Research Foundation [2019ZR13, 2019ZG29]

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A novel highly productive beta-glucosidase strain was isolated from Camptotheca acuminata seeds, showing 14.4-fold increase in activity compared to control. The purified and immobilized beta-glucosidase exhibited enhanced thermal stability, reusability, and substrate specificity, making it a promising alternative for cellulosic ethanol production.
Beta-glucosidase (EC 3.2.1.21) catalyzes the hydrolysis of cellobiose and cellooligosaccharides containing (1 -> 4)-beta-glycosidic bonds to glucose, which is crucial in cellulosic ethanol production. In this study, Aspergillus versicolor, a novel highly productive beta-glucosidase strain, was first isolated from Camptotheca acuminata seeds. The highest beta-glucosidase activitywith 812.86 U/mL was obtained by using the response surface methodology, and a 14.4-fold has increased compared to the control. The beta-glucosidasewas then purified to homogeneity with recovery yield and specific activity of 25.98% and 499.15 U/mg, respectively. To enhance its stability and recyclability, the purified beta-glucosidase was first immobilized onto magnetic MnO2 by electrostatic adsorption. The immobilized materials were characterized by FR-IT, TEM and FE-SEM. Compared with the free beta-glucosidase, the immobilized enzyme exhibited enhanced thermal stability (1.5-fold raise in half-life at 50 degrees C), and reusability (holding over 60% activity after eight cycles), besides, the optimum pH has increased to 6.0. Substrate specificity research suggested that the enzyme had high hydrolytic activity on cellobiose. It also had a hydrolysis effect on (1 -> 3) and (1 -> 6)-beta-glycosidic linkages. Application trials in cellulose hydrolysis revealed that the immobilized enzyme was comparatively more effective. Our results suggested this novel immobilized beta-glucosidase makes a promising alternative for the cellulosic ethanol production. (c) 2021 Elsevier B.V. All rights reserved.

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