Journal Articles
- Development of a Novel D‑Lactic Acid Production Platform Based on Lactobacillus saerimneri TBRC 5746
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Kitisak Sansatchanon , Pipat Sudying , Peerada Promdonkoy , Yutthana Kingcha , Wonnop Visessanguan , Sutipa Tanapongpipat , Weerawat Runguphan , Kanokarn Kocharin
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J. Microbiol. 2023;61(9):853-863. Published online September 14, 2023
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DOI: https://doi.org/10.1007/s12275-023-00077-x
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4
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Abstract
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D-Lactic acid is a chiral, three-carbon organic acid, that bolsters the thermostability of polylactic acid. In this study, we
developed a microbial production platform for the high-titer production of D-lactic acid. We screened 600 isolates of lactic
acid bacteria (LAB) and identified twelve strains that exclusively produced D-lactic acid in high titers. Of these strains,
Lactobacillus saerimneri TBRC 5746 was selected for further development because of its homofermentative metabolism.
We investigated the effects of high temperature and the use of cheap, renewable carbon sources on lactic acid production and
observed a titer of 99.4 g/L and a yield of 0.90 g/g glucose (90% of the theoretical yield). However, we also observed L-lactic
acid production, which reduced the product’s optical purity. We then used CRISPR/dCas9-assisted transcriptional repression
to repress the two Lldh genes in the genome of L. saerimneri TBRC 5746, resulting in a 38% increase in D-lactic acid
production and an improvement in optical purity. This is the first demonstration of CRISPR/dCas9-assisted transcriptional
repression in this microbial host and represents progress toward efficient microbial production of D-lactic acid.
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- Industrial–scale production of various bio–commodities by engineered microbial cell factories: Strategies of engineering in microbial robustness
Ju-Hyeong Jung, Vinoth Kumar Ponnusamy, Gopalakrishnan Kumar, Bartłomiej Igliński, Vinod Kumar, Grzegorz Piechota
Chemical Engineering Journal.2024; 502: 157679. CrossRef - Microbial Cell Factories: Biodiversity, Pathway Construction, Robustness, and Industrial Applicability
Rida Chaudhary, Ali Nawaz, Mireille Fouillaud, Laurent Dufossé, Ikram ul Haq, Hamid Mukhtar
Microbiology Research.2024; 15(1): 247. CrossRef - Adaptive Evolution for the Efficient Production of High-Quality d-Lactic Acid Using Engineered Klebsiella pneumoniae
Bo Jiang, Jiezheng Liu, Jingnan Wang, Guang Zhao, Zhe Zhao
Microorganisms.2024; 12(6): 1167. CrossRef - Enhancing D-lactic acid production from non-detoxified corn stover hydrolysate via innovative F127-IEA hydrogel-mediated immobilization of Lactobacillus bulgaricus T15
Yuhan Zheng, Feiyang Sun, Siyi Liu, Gang Wang, Huan Chen, Yongxin Guo, Xiufeng Wang, Maia Lia Escobar Bonora, Sitong Zhang, Yanli Li, Guang Chen
Frontiers in Microbiology.2024;[Epub] CrossRef
- Proteome analysis reveals global response to deletion of mrflbA in Monascus ruber
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Qingqing Yan , Zhouwei Zhang , Yishan Yang , Fusheng Chen , Yanchun Shao
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J. Microbiol. 2018;56(4):255-263. Published online February 28, 2018
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DOI: https://doi.org/10.1007/s12275-018-7425-8
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46
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Abstract
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Monascus spp. are commonly used for a wide variety of applications
in the food and pharmaceutical industries. In previous
studies, the knock-out of mrflbA (a putative regulator
of the G protein α subunit) in M. ruber led to autolysis of
the mycelia, decreased pigmentation and lowered mycotoxin
production. Therefore, we aimed to obtain a comprehensive
overview of the underlying mechanism of mrflbA deletion
at the proteome level. A two-dimensional gel electrophoresis
analysis of mycelial proteins indicated that the abundance
of 178 proteins was altered in the ΔmrflbA strain, 33 of which
were identified with high confidence. The identified proteins
are involved in a range of activities, including carbohydrate
and amino acid metabolism, hyphal development and the oxidative
stress response, protein modification, and the regulation
of cell signaling. Consistent with these findings, the activity
of antioxidative enzymes and chitinase was elevated in
the supernatant of the ΔmrflbA strain. Furthermore, deletion
of mrflbA resulted in the transcriptional reduction of secondary
metabolites (pigment and mycotoxin). In short, the
mutant phenotypes induced by the deletion of mrflbA were
consistent with changes in the expression levels of associated
proteins, providing direct evidence of the regulatory functions
mediated by mrflbA in M. ruber.
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- Histone deacetylase MrHos3 negatively regulates the production of citrinin and pigments in Monascus ruber
Qianrui Liu, Yunfan Zheng, Baixue Liu, Fufang Tang, Yanchun Shao
Journal of Basic Microbiology.2023; 63(10): 1128. CrossRef - Histone deacetylase MrRpd3 plays a major regulational role in the mycotoxin production of Monascus ruber
Yunfan Zheng, Yueyan Huang, Zejing Mao, Yanchun Shao
Food Control.2022; 132: 108457. CrossRef - Characterization of key upstream asexual developmental regulators in Monascus ruber M7
Lili Jia, Yuyun Huang, Jae-Hyuk Yu, Marc Stadler, Yanchun Shao, Wanping Chen, Fusheng Chen
Food Bioscience.2022; 50: 102153. CrossRef - Quantitative Proteomics Analysis by Sequential Window Acquisition of All Theoretical Mass Spectra–Mass Spectrometry Reveals Inhibition Mechanism of Pigments and Citrinin Production of Monascus Response to High Ammonium Chloride Concentration
Bo Zhou, Yifan Ma, Yuan Tian, Jingbo Li, Haiyan Zhong
Journal of Agricultural and Food Chemistry.2020; 68(3): 808. CrossRef
Research Support, Non-U.S. Gov't
- The Changes of Proteomes Components of Helicobacter pylori in Response to Acid Stress without Urea
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Chunhong Shao , Qunye Zhang , Wei Tang , Wei Qu , Yabin Zhou , Yundong Sun , Han Yu , Jihui Jia
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J. Microbiol. 2008;46(3):331-337. Published online July 5, 2008
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DOI: https://doi.org/10.1007/s12275-008-0062-x
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Scopus
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Abstract
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Acid stress is the most obvious challenge Helicobacter pylori encounters in human stomach. The urease system is the basic process used to maintain periplasmic and cytoplasmic pH near neutrality when H. pylori is exposed to acidic condition. However, since the urea concentration in gastric juice is approximately 1 mM, considered possibly insufficient to ensure the survival of H. pylori, it is postulated that additional mechanisms of pH homeostasis may contribute to the acid adaptation in H. pylori. In order to identify the acid-related proteins other than the urease system we have compared the proteome profiles of H. pylori strain 26695 exposed to different levels of external pH (7.4, 6.0, 5.0, 4.0, 3.0, and 2.0) for 30 min in the absence of urea using 2-DE. Differentially expressed proteins were identified by MALDI-TOF-TOF-MS analysis, which turned out to be 36 different proteins. The functions of these proteins included ammonia production, molecular chaperones, energy metabolism, cell envelope, response regulator and some proteins with unknown function. SOM analysis indicated that H. pylori responds to acid stress through multi-mechanisms involving many proteins, which depend on the levels of acidity the cells encounter.