Abstract

Alkaline polygalacturonate lyase (PGL, EC 4.2.2.2) can catalyze the cleavage of a-1, 4-glycosidic bonds of polygalacturonate by a trans-elimination reaction and generate an unsaturated oligogalacturonates. As the critical enzyme of many environmental friendly processes, alkaline PGL has been widely used in many fields including paper, textile and beverage industries. At present, Bacillus subtilis is an ideal strain for producing PGL, but the yield is too low for industrial production. In this study, the effect of different SD sequences on the production of PGL was comparatively investigated, and the strong SD sequence (AGAGAACAAGGAGGG G) directed efficient PGL secretory expression and increased PGL yield to 264.5 U·mL-1 with a high productivity. As a result, the PGL yield in B. subtilis was effecively increased and laid the solid foundation for PGL industrial production.

Details

Title
High PGL productivity in Bacillus subtilis by optimizing the SD sequence
Author
Zhang, Junjiao
Section
Environmental Ecological Analysis and Sustainable Development Research
Publication year
2021
Publication date
2021
Publisher
EDP Sciences
ISSN
25550403
e-ISSN
22671242
Source type
Conference Paper
Language of publication
English
ProQuest document ID
2577561394
Copyright
© 2021. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and conditions, you may use this content in accordance with the terms of the License.