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Multi-stage glucose/pachymaran co-feeding enhanced endo-β-1,3-glucanase production by Trichoderma harzianum via simultaneous increases in cell concentration and inductive effect.

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Title: Multi-stage glucose/pachymaran co-feeding enhanced endo-β-1,3-glucanase production by Trichoderma harzianum via simultaneous increases in cell concentration and inductive effect.
Authors: Gao, Min-Jie1 (AUTHOR), Liu, Li-Ping1 (AUTHOR), Li, Shan1 (AUTHOR), Lyu, Ji-Liang2 (AUTHOR), Jiang, Yun1 (AUTHOR), Zhu, Li3 (AUTHOR), Zhan, Xiao-Bei1 (AUTHOR) xbzhan@yahoo.com, Zheng, Zhi-Yong1,4 (AUTHOR)
Source: Bioprocess & Biosystems Engineering. Aug2020, Vol. 43 Issue 8, p1479-1486. 8p.
Subjects: Inductive effect, Trichoderma harzianum, Glucose, Polysaccharides, Cell growth, Manufacturing processes
Abstract: Endo-β-1,3-glucanase is used to hydrolyze curdlan in a wide range of oligosaccharides production processes. Using pachymaran as the sole carbon source resulted in an endo-β-1,3-glucanase activity of 86.1 U/mL and an Eendo/Etotal ratio of 0.43, which were 3.2 and 1.65 folds of the values from control (glucose as the sole carbon source), due to the inductive effect of pachymaran as a polysaccharide. However, the cell concentration decreased from 25 to 12 g/L during the late fermentation phase. Therefore, a novel multi-stage feeding strategy was developed wherein glucose was fed twice during the cell logarithmic growth phase (24 and 48 h) and pachymaran once during the early stage of the enzyme accumulation phase (72 h). Consequently, the cell concentration remained around 30 g/L during the late fermentation phase. Endo-β-1,3-glucanase activity and Eendo/Etotal reached 160.0 U/mL and 0.76, respectively, which were 6.0 and 2.92 folds of the values from control. In addition, three typical polysaccharides with β-1,3-linked glucose residues were successfully hydrolyzed by endo-β-1,3-glucanase to produce multifunctional β-1,3-oligoglucosides. [ABSTRACT FROM AUTHOR]
Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Multi-stage glucose/pachymaran co-feeding enhanced endo-β-1,3-glucanase production by Trichoderma harzianum via simultaneous increases in cell concentration and inductive effect.
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  Data: <searchLink fieldCode="JN" term="%22Bioprocess+%26+Biosystems+Engineering%22">Bioprocess & Biosystems Engineering</searchLink>. Aug2020, Vol. 43 Issue 8, p1479-1486. 8p.
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  Data: Endo-β-1,3-glucanase is used to hydrolyze curdlan in a wide range of oligosaccharides production processes. Using pachymaran as the sole carbon source resulted in an endo-β-1,3-glucanase activity of 86.1 U/mL and an Eendo/Etotal ratio of 0.43, which were 3.2 and 1.65 folds of the values from control (glucose as the sole carbon source), due to the inductive effect of pachymaran as a polysaccharide. However, the cell concentration decreased from 25 to 12 g/L during the late fermentation phase. Therefore, a novel multi-stage feeding strategy was developed wherein glucose was fed twice during the cell logarithmic growth phase (24 and 48 h) and pachymaran once during the early stage of the enzyme accumulation phase (72 h). Consequently, the cell concentration remained around 30 g/L during the late fermentation phase. Endo-β-1,3-glucanase activity and Eendo/Etotal reached 160.0 U/mL and 0.76, respectively, which were 6.0 and 2.92 folds of the values from control. In addition, three typical polysaccharides with β-1,3-linked glucose residues were successfully hydrolyzed by endo-β-1,3-glucanase to produce multifunctional β-1,3-oligoglucosides. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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