Silage pathogens and biological control agents: effects, action mechanisms, challenges and prospects

Jiang, Huifang; Okoye, Charles Obinwanne; Wu, Yanfang; Gao, Lu; Li, Xia; Wang, Yongli; Jiang, Jianxiong

doi:10.1007/s10526-023-10236-z

Cited by 1 publication

(1 citation statement)

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“…Lactic acid bacteria that heterologously express OXDC may be used as potential probiotics for degrading intestinal oxalate to prevent calcium oxalate (CaOx) stone (Figure ). − For example, Paul and his colleagues developed food-grade probiotic L. plantarum secreting OXDC using mobile genetic element Ll.LtrB and chromosomal integration, which is capable of degrading intestinal oxalate and preventing CaOx stone formation in experimental rats. , Wu et al found that Zn 2+ regulates human oxalate metabolism by manipulating oxalate decarboxylase to treat calcium oxalate stones and promoting Lactobacillus in the intestinal flora . More interesting is that Human Embryonic Kidney 293 (HEK293) cells expressing OXDC are capable of degrading oxalate protect cells from oxidative damage and serve as a therapeutic option for prevention of CaOx stone disease …”

Section: Application Of Oxalate Decarboxylasementioning

confidence: 99%

Recent Advances of Oxalate Decarboxylase: Biochemical Characteristics, Catalysis Mechanisms, and Gene Expression and Regulation

Zan,

Yan,

Chen

et al. 2024

J. Agric. Food Chem.

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Oxalate decarboxylase (OXDC) is a typical Mn 2+ /Mn 3+ dependent metal enzyme and splits oxalate to formate and CO 2 without any organic cofactors. Fungi and bacteria are the main organisms expressing the OXDC gene, but with a significantly different mechanism of gene expression and regulation. Many articles reported its potential applications in the clinical treatment of hyperoxaluria, low-oxalate food processing, degradation of oxalate salt deposits, oxalate acid diagnostics, biocontrol, biodemulsifier, and electrochemical oxidation. However, some questions still remain to be clarified about the role of substrate binding and/or protein environment in modulating the redox properties of enzyme-bound Mn(II)/Mn(III), the nature of dioxygen involved in the catalytic mechanism, and how OXDC acquires Mn(II) /Mn(III). This review mainly summarizes its biochemical and structure characteristics, gene expression and regulation, and catalysis mechanism. We also deep-mined oxalate decarboxylase gene data from National Center for Biotechnology Information to give some insights to explore new OXDC with diverse biochemical properties.

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