4.4 Article

Using One-pot Fermentation Technology to Prepare Enzyme Cocktail to Sustainably Produce Low Molecular Weight Galactomannans from Sesbania cannabina Seeds

Journal

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
Volume 194, Issue 7, Pages 3016-3030

Publisher

SPRINGER
DOI: 10.1007/s12010-022-03891-y

Keywords

Galactomannans; beta-mannanase; alpha-galactosidase; Enzyme hydrolysis; Low molecular weight galactomannans

Funding

  1. National Key R&D Program of China [2016YFD0600803]
  2. Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD)

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This study investigated the production of low molecular weight galactomannan (LMW-GM) from leguminous seeds using enzymatic hydrolysis. The researchers used a one-pot fermentation technology to cultivate Trichoderma reesei with a cocktail of beta-mannanase and alpha-galactosidase. The results showed that a combination of avicel and melibiose as carbon sources resulted in an enzyme cocktail with high activities of beta-mannanase and alpha-galactosidase. The use of melibiose effectively induced the production of alpha-galactosidase, which improved the degradation of galactose in GM and increased the yield of LMW-GM.
Enzymatic hydrolysis using beta-mannanase and alpha-galactosidase is necessary to produce low molecular weight galactomannan (LMW-GM) from galactomannans (GM) in the leguminous seeds. In this study, different ratios of avicel and melibiose were used as the inductors (carbon sources) for Trichoderma reesei to metabolize the enzyme cocktail containing beta-mannanase and alpha-galactosidase using one-pot fermentation technology. The obtained enzyme cocktail was used to efficiently produce LMW-GM from GM in Sesbania cannabina seeds. Results showed that 15 g/L avicel and 10 g/L melibiose were the best carbon sources to prepare enzyme cocktail containing beta-mannanase and alpha-galactosidase with activities of 3.69 +/- 0.27 U/mL and 0.51 +/- 0.02 U/mL, respectively. Specifically, melibiose could effectively induce the metabolite product of alpha-galactosidase by T. reesei, which showed good performance in degrading the galactose substituent from GM backbone. The degradation of galactose alleviated the spatial site-blocking effect for enzymatic hydrolysis by beta-mannanase and improved the yield of LMW-GM. This research can lay the foundation for the industrial technology amplification of LMW-GM production for further application.

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