AI Article Synopsis
- The xyloglucanase gene (RmXEG12A) from the fungus Rhizomucor miehei was successfully expressed in the yeast Pichia pastoris, showing a high enzyme activity of 25,700 U/mL through high cell density fermentation.
- The enzyme performs best at pH 7.0 and a temperature of 65 °C, specifically breaking down xyloglucan with a notable activity rate.
- Hydrolysis of tamarind powder produced xyloglucan oligosaccharides, which enhanced the water holding capacity of yogurt and significantly promoted the growth of beneficial bacteria in the yogurt.
Article Abstract
The xyloglucanase gene (RmXEG12A) from Rhizomucor miehei CAU432 was successfully expressed in Pichia pastoris. The highest xyloglucanase activity of 25,700 U mL was secreted using high cell density fermentation. RmXEG12A was optimally active at pH 7.0 and 65 °C, respectively. The xyloglucanase exhibited the highest specific activity towards xyloglucan (7915.5 U mg). RmXEG12A was subjected to hydrolyze tamarind powder to produce xyloglucan oligosaccharides with the degree of polymerization (DP) 7-9. The hydrolysis ratio of xyloglucan in tamarind powder was 89.8%. Moreover, xyloglucan oligosaccharides (2.0%, w/w) improved the water holding capacity (WHC) of yoghurt by 1.1-fold and promoted the growth of Lactobacillus bulgaricus and Streptococcus thermophiles by 2.3 and 1.6-fold, respectively. Therefore, a suitable xyloglucanase for tamarind powder hydrolysis was expressed in P. pastoris at high level and xyloglucan oligosaccharides improved the quality of yoghurt.
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| http://dx.doi.org/10.1016/j.ijbiomac.2021.09.035 | DOI Listing |
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