Aims: Bacillus licheniformis AQ is an industrial strain with high production of alkaline protease (AprE), which has great industrial application value. However, how to regulate the production of AprE in the process of industrial fermentation is still not completely clear. Therefore, it is important to understand the metabolic process of AprE production in the industrial fermentation medium.
Methods And Results: In this study, transcriptome sequencing of the whole fermentation course was performed to explore the synthesis and regulation mechanism of AprE in B. licheniformis AQ. During the fermentation process, the AprE got continuously accumulated, reaching a peak of 42 020 U/mL at the fermentation endpoint (48 h). Meanwhile, the highly expressed genes were observed. Compared with the fermentation endpoint, there were 61 genes in the intersection of differentially expressed genes, functioning as catabolic processes, peptidases and inhibitors, chaperones, and folding catalysts. Furthermore, the protein-protein interactions network of AprE was constructed.
Conclusion: This study provides important transcriptome information for B. licheniformis AQ and potential molecular targets for further improving the production of AprE.
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http://dx.doi.org/10.1093/jambio/lxad319 | DOI Listing |
Animals (Basel)
January 2025
State Key Laboratory of Animal Nutrition and Feeding, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
infection can induce necrotic enteritis and lead to significant economic loss to the chicken industry. In this study, a xylanase (Xyn10C), which effectively promotes the growth of probiotics, and a protease, which degrades the biofilm of were analyzed for their ability to alleviate -induced necrotic enteritis in broiler chickens. A total of 300 male AA chickens were divided into five treatment groups (control, no enzyme and no challenge; Cp, no enzyme, challenge; Xyn, Xyn10C plus challenge; Xyn+Am, Xyn10C+Amylase plus challenge; Xyn+Ap, Xyn10C+Alkaline protease plus challenge).
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Nitte (Deemed to be University), Nitte University Centre for Science Education and Research, Department of Bio & Nano Technology, Paneer Campus, Deralakatte, Mangaluru 575018, Karnataka, India. Electronic address:
Bacteriophages, the most abundant biological agents targeting bacteria, offer a promising alternative to antibiotics for combating multi-drug resistant pathogens like Acinetobacter baumannii. However, the rapid development of bacteriophage resistance poses a significant challenge. This study highlights the contribution of outer membrane proteins (OMPs) in the emergence of bacteriophage resistance in A.
View Article and Find Full Text PDFFood Chem
January 2025
Department of Molecular Biology and Genetics, Faculty of Science, Ataturk University, 25240, Erzurum, Turkey. Electronic address:
Recycling of protein-rich environmental wastes and obtaining more valuable products from these recycled products is a topic of interest for researchers. This study aims to produce, purify, and characterize the physicochemical and structural properties of the protease enzyme produced from Brevibacillus agri SAR25 using salmon fish waste as substrate and also to evaluate the effect of protease on the chicken feather, enzyme-ligand interactions, and active site surface area. The production of protease was optimum on 50 g/L fish waste, pH 8, 40 °C, 96 h, and 150 rpm.
View Article and Find Full Text PDFArch Dermatol Res
January 2025
Department of Biotechnology, Institute of Graduate Studies and Research, Alexandria University, Alexandria, 21526, Egypt.
J Fungi (Basel)
December 2024
College of Food Sciences and Technology, Shanghai Ocean University, Shanghai 201306, China.
is a tasty and low-calorie mushroom containing abundant high-quality protein. This study aims to improve the digestibility of protein (PEP) and hence to facilitate its development as a healthy alternative protein. The extracted PEP was pretreated with 1000-5000 U of papain, neutral protease and alkaline protease.
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