A reverse catalytic triad Asp containing loop shaping a wide substrate binding pocket of a feruloyl esterase from Lactobacillus plantarum

Zhang, Haowen; Wen, Bin; Liu, Yusi; Du, Guoming; Wei, Xue; Imam, Khandaker Md Sharif Uddin; Zhou, Huan; Fan, Shilong; Wang, Fengzhong; Wang, Yulu; Xin, Fengjiao

doi:10.1016/j.ijbiomac.2021.06.033

Cited by 11 publications

(5 citation statements)

References 43 publications

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“…The bound phenolics in barley are mainly bonded with DFs through ester bonds, 2 where feruloyl esterase from Lactobacillus plantarum can break the ester bond cross-linked between the polysaccharide side chain of hemicellulose and ferulic acid in plant cell walls, thus improving the release of bound phenolics. 32 Compared to the undigested RBDF, the signal significantly decreased in the undigested FBDF residue, which confirmed that Lp. plantarum dy-1 fermentation enhanced the liberation of bound phenolics.…”

Section: Resultssupporting

confidence: 58%

Changes in the structural, physicochemical and functional properties and in vitro fecal fermentation characteristics of barley dietary fiber fermented by Lactiplantibacillus plantarum dy-1

Xiao,

Li,

Bai

et al. 2024

Food Funct.

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Section: Resultssupporting

confidence: 58%

Changes in the structural, physicochemical and functional properties and in vitro fecal fermentation characteristics of barley dietary fiber fermented by Lactiplantibacillus plantarum dy-1

Xiao,

Li,

Bai

et al. 2024

Food Funct.

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“…FAEs of fungal origin are currently the best characterized, and of considerable industrial interest ( Dilokpimol et al, 2016 ; Underlin et al, 2020 ). However, several bacterial FAEs have also been characterized structurally and biochemically, including the FAEs from Clostridium thermocellum ( Tabouriech et al, 2005 ), Dickeya dadantii ( Hassan and Hugouvieux-Cotte-Pattat, 2011 ), Lactobacilli and Bifidobacteria ( Lai et al, 2011 ; Fritsch et al, 2017 ; Xu et al, 2017 ; Zhang et al, 2021 ), Butyrivibrio proteoclasticus ( Goldstone et al, 2010 ), Bacteroides intenstinalis ( Pereira et al, 2021 ), Streptomyces cinnamoneus ( Uraji et al, 2018 ), and uncultured bacteria from metagenomic studies ( Holck et al, 2019 ).…”

Section: Introductionmentioning

confidence: 99%

“…In addition to having beneficial effects on the human and animal intestinal tracts ( Wang et al, 2004 ; Liu et al, 2021 ), these bacteria also play an important role in silage fermentation, which relies on the production of organic acids to inhibit the growth of unwanted microorganisms ( Mogodiniyai Kasmaei et al, 2020 ). Several LABs demonstrate high FAE activity, including L. acidophilus , L. amylovorus , L. farciminis , L. fermentum , L. gasseri , L. helveticus , L. johnsonii , and L. reuteri , L. farciminis , L. reuteri , and L. crispatus ( Wang et al, 2004 ; Lai et al, 2011 ; Esteban-Torres et al, 2013 ; Xu et al, 2020 ; Liu et al, 2021 ; Zhang et al, 2021 ), but few studies have investigated the structural basis of the substrate binding and catalytic mechanisms.…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state

et al. 2022

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Ferulic acid is a common constituent of the plant cell-wall matrix where it decorates and can crosslink mainly arabinoxylans to provide structural reinforcement. Microbial feruloyl esterases (FAEs) specialize in catalyzing hydrolysis of the ester bonds between phenolic acids and sugar residues in plant cell-wall polysaccharides such as arabinoxylan to release cinnamoyl compounds. Feruloyl esterases from lactic acid bacteria (LAB) have been highlighted as interesting enzymes for their potential applications in the food and pharmaceutical industries; however, there are few studies on the activity and structure of FAEs of LAB origin. Here, we report the crystal structure and biochemical characterization of a feruloyl esterase (LbFAE) from Lentilactobacillus buchneri, a LAB strain that has been used as a silage additive. The LbFAE structure was determined in the absence and presence of product (FA) and reveals a new type of homodimer association not previously observed for fungal or bacterial FAEs. The two subunits associate to restrict access to the active site such that only single FA chains attached to arabinoxylan can be accommodated, an arrangement that excludes access to FA cross-links between arabinoxylan chains. This narrow specificity is further corroborated by the observation that no FA dimers are produced, only FA, when feruloylated arabinoxylan is used as substrate. Docking of arabinofuranosyl-ferulate in the LbFAE structure highlights the restricted active site and lends further support to our hypothesis that LbFAE is specific for single FA side chains in arabinoxylan.

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“…In some cases, it is used to clarify the relationship between protein structure and properties and is considered a powerful tool to modify DNA sequences in molecular biological studies and genetic engineering [ 34 ]. Haowen Zhang et al rationally increased 4- and 5-fold catalytic efficiency of a feruloyl esterase LP_0796 from Lactobacillus plantarum by mutation Asp with Ala23 and Ile198, respectively [ 35 ]. Eight mutants were generated based on the simulated structure to enhance the catalytic efficiency of a feruloyl esterase FAELac, among which Q198A and Q134T were enhanced by 5.4- and 4.3-fold catalytic efficiencies, respectively, in comparison with WT [ 36 ].…”

Section: Discussionmentioning

confidence: 99%

Enhancing the Hydrolysis and Acyl Transfer Activity of Carboxylesterase DLFae4 by a Combinational Mutagenesis and In-Silico Method

Ding

Shao

et al. 2023

Foods

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In the present study, a feruloyl esterase DLFae4 identified in our previous research was modified by error-prone PCR and site-directed saturation mutation to enhance the catalytic efficiency and acyltransferase activity further. Five mutants with 6.9–118.9% enhanced catalytic activity toward methyl ferulate (MFA) were characterized under the optimum conditions. Double variant DLFae4-m5 exhibited the highest hydrolytic activity (270.97 U/mg), the Km value decreased by 83.91%, and the Kcat/Km value increased by 6.08-fold toward MFA. Molecular docking indicated that a complex hydrogen bond network in DLFae4-m5 was formed, with four of five bond lengths being shortened compared with DLFae4, which might account for the increase in catalytic activity. Acyl transfer activity assay revealed that the activity of DLFae4 was as high as 1550.796 U/mg and enhanced by 375.49% (5823.172 U/mg) toward 4-nitrophenyl acetate when residue Ala-341 was mutated to glycine (A341G), and the corresponding acyl transfer efficiency was increased by 7.7 times, representing the highest acyltransferase activity to date, and demonstrating that the WGG motif was pivotal for the acyltransferase activity in family VIII carboxylesterases. Further experiments indicated that DLFae4 and variant DLFae4 (A341G) could acylate cyanidin-3-O-glucoside effectively in aqueous solution. Taken together, our study suggested the effectiveness of error-prone PCR and site-directed saturation mutation to increase the specific activity of enzymes and may facilitate the practical application of this critical feruloyl esterase.

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A reverse catalytic triad Asp containing loop shaping a wide substrate binding pocket of a feruloyl esterase from Lactobacillus plantarum

Cited by 11 publications

References 43 publications

Changes in the structural, physicochemical and functional properties and in vitro fecal fermentation characteristics of barley dietary fiber fermented by Lactiplantibacillus plantarum dy-1

Changes in the structural, physicochemical and functional properties and in vitro fecal fermentation characteristics of barley dietary fiber fermented by Lactiplantibacillus plantarum dy-1

Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state

Enhancing the Hydrolysis and Acyl Transfer Activity of Carboxylesterase DLFae4 by a Combinational Mutagenesis and In-Silico Method

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