A novel amidase from <i>Brevibacterium epidermidis</i> ZJB-07021: gene cloning, refolding and application in butyrylhydroxamic acid synthesis

Ruan, Li-Tao; Zheng, Ren‐Chao; Zheng, Yu‐Guo

doi:10.1007/s10295-016-1786-y

Cited by 15 publications

(4 citation statements)

References 45 publications

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“…The IBs of SoP5CS were firstly purified by Ni-NTA Resin and about 15 mg purified SoP5CS was obtained from 1 liter of culture broth after refolding, dialysis, gel filtration and concentration. The yield of SoP5CS was not very high compared with other proteins purified from inclusion body (Ruan et al, 2016), but it was enough for further use.…”

Section: Discussionmentioning

confidence: 93%

Preparation and Application of Monoclonal Antibody to Sugarcane (Saccharum L. Spp. Hybrids) Sop5cs Protein

Li¹

2019

Appl. Ecol. Env. Res.

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△ 1 -pyrroline-5-carboxylate synthase (P5CS) is a key enzyme in proline biosynthesis. In this study, the nucleotide sequence of sugarcane P5CS (SoP5CS) gene was obtained from sugarcane. Then the ORF of SoP5CS linked with pET-30a vector and the SoP5CS protein was expressed successfully in E. coli by the induction of 1.0 mM IPTG at 28 °C for 6 h. The prokaryotic expression protein was expressed as inclusion bodies (IBs). It was purified by Ni-NTA Resin firstly and then refolded, dialyzed and further purified by gel filtration. The monoclonal antibody of SoP5CS was prepared using mice. The expression of SoP5CS gene and the corresponding protein and physiological parameters associated with drought resistance were detected in sugarcane leaves under different drought stresses, they worked together to regulate the drought resistance process of sugarcane. This is the first report on the preparation of P5CS monoclonal antibody and the expression of the antibody in sugarcane, which would provide new methods to study the function of SoP5CS response to various abiotic stresses and other aspects.

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Section: Discussionmentioning

confidence: 93%

Preparation and Application of Monoclonal Antibody to Sugarcane (Saccharum L. Spp. Hybrids) Sop5cs Protein

Li¹

2019

Appl. Ecol. Env. Res.

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“…Ruan et al . (2016) reported Brevibacterium epidermidis ZJB‐07021 for butyrylhydroxamic acid synthesis. In the existing literature, it was observed that there is no report available on the biotransformation of complex amide to pharmaceutically important hydroxamic acid i.e., N ‐hydroxy‐ N ′‐phenyloctanediamide (Vorinostat).…”

Section: Discussionmentioning

confidence: 99%

Novel amidase catalysed process for the synthesis of vorinostat drug

et al. 2020

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Aim Presently, N‐hydroxy‐N′‐phenyloctanediamide (vorinostat) which is an effective histone deacetylase inhibitor, is being synthesized chemically. Hence, present study aims to develop an eco‐friendly approach for the synthesis of vorinostat from N′‐phenyloctanediamide through biotransformation. Methods and Results Using the amidase of Bacillus smithii IIIMB2907 in time course conversion and organic solvent compatibility, maximum bioconversion was observed at 12 h of reaction time and in presence of ethanol, respectively. Potassium phosphate buffer of pH 7·0 supported maximum bioconversion of N′‐phenyloctanediamide (10 mmol l−1) into N‐hydroxy‐N′‐ phenyloctanediamide at 40°C. Bench scale study was successfully carried out with 83% yield of purified vorinostat. Conclusion In this study, an eco‐friendly approach for the biotransformation of N′‐phenyloctanediamide into vorinostat was developed by using cell free extract of thermophilic strain B. smithii IIIMB2907. Significance and Impact of the Study Microbial amidase has achieved remarkable attention in the field of biotransformation for the green synthesis of hydroxamic acids. Utilization of amidase from B. smithii IIIMB2907, specifically in the synthesis of vorinostat drug is a foremost attempt in the development a novel process and can also be employed in the synthesis of its derivatives as well.

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“…Ruan and co‐workers cloned and expressed a novel amidase gene ( bami ) from Brevibacterium epidermidis ZJB 07021 in E. coli and utilized it for the synthesis of butyrohydroxamic acid (Scheme4f) from butyramide. The strain showed an 88.1 % yield of butyrohydroxamic acid after 15 min of incubation under optimized conditions 14.…”

Section: Methods For Hydroxamic Acid Synthesismentioning

confidence: 99%

“…However, few enzymatic processes have been developed involving the use of nicotinic hydroxamate, benzohydroxamic acid, acetohydroxamic acid, butyrohydoxamic acid, etc. [10][11][12][13][14][15]. Till 2020, only simple-structured hydroxamic acids were reported and no complex structured hydroxamic acids were known due to the unavailability of a corresponding substrate for hydroxamic -----acid.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Catalysts for Hydroxamic Acid Formation: A Mini‐Review

Singh

2023

ChemBioEng Reviews

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In recent years, biocatalysts have emerged as crucial tool in organic synthesis, particularly for the production of drug intermediates and precursors, e.g., the synthesis of hydroxamic acids. Traditionally, hydroxamic acids were synthesized using organic chemistry methods. However, with the growing emphasis on sustainable and environment‐friendly practices, the chemical industry has increasingly turned towards green synthesis approaches. The significance of hydroxamic acids in medicinal chemistry has also contributed to the changing trends. Following the approval of certain hydroxamic acids as histone deacetylase (HDAC) inhibitors for cancer treatment by the Food and Drug Administration (US‐FDA), there has been a renewed focus on their synthesis and the development of derivatives with improved properties. As an alternative route, amidases have emerged as promising biocatalysts for hydroxamic acid synthesis through their acyltransferase activity. Recent advancements in the synthesis approaches for hydroxamic acids are reviewed. The biocatalytic routes are explored, emphasizing the use of amidases and their acyltransferase activity. The scope and potential applications of this chemoenzymatic approach in synthesizing various hydroxamic acids and their derivatives are discussed. Such advancements have the potential to revolutionize the production of these important compounds, making the synthesis process more sustainable, efficient, and economically viable.

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A novel amidase from Brevibacterium epidermidis ZJB-07021: gene cloning, refolding and application in butyrylhydroxamic acid synthesis

Cited by 15 publications

References 45 publications

Preparation and Application of Monoclonal Antibody to Sugarcane (Saccharum L. Spp. Hybrids) Sop5cs Protein

Preparation and Application of Monoclonal Antibody to Sugarcane (Saccharum L. Spp. Hybrids) Sop5cs Protein

Novel amidase catalysed process for the synthesis of vorinostat drug

Enzymatic Catalysts for Hydroxamic Acid Formation: A Mini‐Review

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