Biological detoxification of fumonisin by a novel carboxylesterase from Sphingomonadales bacterium and its biochemical characterization

Li, Zhongyuan; Wang, Yan; Liu, Zhongqi; Jin, Shanzheng; Pan, Kungang; Liu, Huihui; Liu, Tianhui; Li, Xiumei; Luo, Xue‐Gang; Song, Yajian; Zhao, Junqi; Zhang, Tongcun

doi:10.1016/j.ijbiomac.2020.12.033

Cited by 33 publications

(25 citation statements)

References 32 publications

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“…This is witnessed in the work by Dellafiora and colleagues (49), where two related, AF-degrading hydrolases shared only 72% sequence similarity, despite using the same mechanism for degradation. In a more extreme example, a recently identified carboxylesterase that degrades fumonisin shows only around 34% sequence similarity to previously reported fumonisindegrading carboxylesterases (50).…”

Section: Finding Candidate Organisms: Who Can Do the Job?mentioning

confidence: 75%

Computational biology for enzymatic removal of mycotoxins

Sandlin¹,

Kish²,

Kim³

et al. 2021

Preprint

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Biological organisms carry a rich potential for removing toxins from our environment, but the search to identify suitable candidates remains challenging. We survey and explore the use of computational tools to discover and optimize the detoxification of harmful compounds. In particular, we will focus on mycotoxins—fungi-produced toxins that contaminate food and feed—and biological enzymes that are capable of rendering them less harmful. We discuss the use of computational tools to complement existing empirical data in three main directions: discovering the prospect of detoxification among underexplored organisms, finding important cellular processes that contribute to detoxification, and optimizing the performance of enzymes with detoxification capability.

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Section: Finding Candidate Organisms: Who Can Do the Job?mentioning

confidence: 75%

Computational biology for enzymatic removal of mycotoxins

Sandlin¹,

Kish²,

Kim³

et al. 2021

Preprint

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“…It was provided by Dr. Zhongyuan Li of Tianjin University of Science and Technology. The primary experiment proved that FumDSB can degrade FB 1 into hydrolyzed fumonisin B 1 (HFB 1 ) by releasing two tricarballylic acid groups, and that the degradation rate can reach 100% [16].…”

Section: Source and Pre-processing Of Fumonisin Detoxification Enzymes Fumdsbmentioning

confidence: 99%

“…Purified FumDSB showed the strongest ability to destroy FB 1 at pH 6.0, and exhibited favorable stability in a wide range of pH, from 4.0 to 9.0. In addition, the optimum operating temperature of FumDSB was 30 • C, and the relative activities of 67.33% and 34.73% were maintained at 37 • C and 40 • C, respectively [16]. In view of its excellent pH stability and moderate thermal stability, FumDSB is very suitable for use under animal physiological conditions.…”

Section: Introductionmentioning

confidence: 99%

“…Since then, increasing numbers of live bacteria or biological enzymes designed to detoxify FB 1 have been screened and identified [13][14][15]; however there are fewer studies on the detoxification mechanism in vivo of biological enzymes. FumDSB is a new type of carboxylesterase, which can degrade FB 1 to hydrolyzed fumonisin B 1 (HFB 1 ) by releasing two tricarballylic acid groups, thereby reducing the toxicity of FB 1 [16]. Purified FumDSB showed the strongest ability to destroy FB 1 at pH 6.0, and exhibited favorable stability in a wide range of pH, from 4.0 to 9.0.…”

Section: Introductionmentioning

confidence: 99%

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FumDSB Can Reduce the Toxic Effects of Fumonisin B1 by Regulating Several Brain-Gut Peptides in Both the Hypothalamus and Jejunum of Growing Pigs

Liu

Huang

et al. 2021

Toxins

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Fumonisin B1 (FB1) is the most common food-borne mycotoxin produced by the Fusarium species, posing a potential threat to human and animal health. Pigs are more sensitive to FB1 ingested from feed compared to other farmed livestock. Enzymatic degradation is an ideal detoxification method that has attracted much attention. This study aimed to explore the functional characteristics of the carboxylesterase FumDSB in growing pigs from the perspective of brain–gut regulation. A total of 24 growing pigs were divided into three groups. The control group was fed a basal diet, the FB1 group was supplemented with FB1 at 5 mg/kg feed, and the FumDSB group received added FumDSB based on the diet of the FB1 group. After 35 days of animal trials, samples from the hypothalamus and jejunum were analyzed through HE staining, qRT-PCR and immunohistochemistry. The results demonstrated that the ingestion of FB1 can reduce the feed intake and weight gain of growing pigs, indicating that several appetite-related brain-gut peptides (including NPY, PYY, ghrelin and obestatin, etc.) play important roles in the anorexia response induced by FB1. After adding FumDSB as detoxifying enzymes, however, the anorexia effects of FB1 were alleviated, and the expression and distribution of the corresponding brain-gut peptides exhibited a certain degree of regulation. In conclusion, the addition of FumDSB can reduce the anorexia effects of FB1 by regulating several brain-gut peptides in both the hypothalamus and the jejunum of growing pigs.

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“…Recently, several FB 1 detoxification carboxylesterases and their responding coding genes were identified and expressed in different hosts. Carboxylesterase FumDSB from Sphingomonadales bacterium expressed in Escherichia coli ( E. coli ) [ 12 ] and the carboxylesterase FumD from Sphingopyxis sp. MTA144 expressed in Pichia pastoris ( P. pastoris , also known as Komagataella phaffii ) GS115 can degrade FB 1 to hydrolyzed fumonisin B1 (HFB 1 ) and thereby reduce the toxicity significantly [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

Improved Production of Recombinant Carboxylesterase FumDM by Co-Expressing Molecular Chaperones in Pichia pastoris

Jiang

Guan

Liu

et al. 2023

Toxins

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Fumonisins (FBs) are mycotoxins that threaten public health and food safety worldwide. Enzymatic degradation of Fumonisin B1 (FB1) through decarboxylation has attracted much attention, whereas application of FB1 carboxylesterase in detoxification requires more effective expression of the recombinant carboxylesterase. In this study, the carboxylesterase FumDM from Sphingopyxis sp. ASAG22 was codon-optimized and co-expressed with five different molecular chaperones (PDI, CPR5, ERO1, HAC1, and Bip) in order to improve the expression level of FumDM in Pichia pastoris (also known as Komagataella phaffii) GS115. The co-expression of different chaperones caused varying degrees of improvement in FumDM activity for FB1. The enzyme activities of recombinant strains over-expressing PDI and CPR5 reached the highest levels of 259.47 U/mL and 161.34 U/mL, 635% and 357% higher than the original enzyme activity, respectively. Transcriptomic analysis of the two recombinant strains in comparison with the control strain showed that the correct folding of proteins assisted by molecular chaperones played a key role in the improvement of FumDM expression and its enzyme activity. This study demonstrated that co-expression of carboxylesterase FumDM and folding chaperones was an efficient strategy and therefore might inspire new perspectives on the improvement of carboxylesterase for detoxification of FB1.

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Biological detoxification of fumonisin by a novel carboxylesterase from Sphingomonadales bacterium and its biochemical characterization

Cited by 33 publications

References 32 publications

Computational biology for enzymatic removal of mycotoxins

Computational biology for enzymatic removal of mycotoxins

FumDSB Can Reduce the Toxic Effects of Fumonisin B1 by Regulating Several Brain-Gut Peptides in Both the Hypothalamus and Jejunum of Growing Pigs

Improved Production of Recombinant Carboxylesterase FumDM by Co-Expressing Molecular Chaperones in Pichia pastoris

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