The GH5 1,4-β-mannanase from Bifidobacterium animalis subsp. lactis Bl-04 possesses a low-affinity mannan-binding module and highlights the diversity of mannanolytic enzymes

Morrill, Johan; Kulcinskaja, Evelina; Sulewska, Anna Maria; Lahtinen, Sampo J.; Stålbrand, Henrik; Svensson, Birte; Hachem, Maher Abou

doi:10.1186/s12858-015-0055-4

Cited by 37 publications

(42 citation statements)

References 59 publications

(77 reference statements)

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“…However, current knowledge on GHs and systems devoted to β-mannan hydrolysis and utilization is scarce (10, 34). Only a few such studies have been devoted to distinct GHs involved in β-mannan conversion in human gut bacteria (30, 32, 41). Previous initial studies on galactomannan-degrading enzymes in B. ovatus indicated only cell-associated β-mannanase and α-galactosidase activity when grown on guar gum galactomannan (11, 12, 42).…”

Section: Discussionmentioning

confidence: 99%

“…The mixtures were boiled for 5 min to stop the reaction and diluted with Millipore water as follows: 1:100 for oligosaccharides; 1:50 for LBG, KGM, and guar gum; and 1:10 for INM, GGM, partially hydrolyzed guar gum, Avicel, and xylan. The dilutions were analyzed using HPAEC-PAD with a CarboPac PA-200 column (Dionex, Sunnyvale, CA) to determine the product profile, as described by Morrill et al (32). …”

Section: Methodsmentioning

confidence: 99%

“…Conservation is greatest within the −1 subsite where the catalytic residues are positioned. Although several β-mannanases have been characterized, including 3D structures of members of GH26 (23–29) as well as the other two families, only recently have a few studies been published on the characterization of β-mannanases from human gut bacteria (30–32). So far, no crystal structure of a β-mannanase from the human gut microbiota has been determined.…”

Section: Introductionmentioning

confidence: 99%

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Galactomannan Catabolism Conferred by a Polysaccharide Utilization Locus of Bacteroides ovatus

Bågenholm

Reddy

Bouraoui

et al. 2017

Journal of Biological Chemistry

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156

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A recently identified polysaccharide utilization locus (PUL) from Bacteroides ovatus ATCC 8483 is transcriptionally up-regulated during growth on galacto- and glucomannans. It encodes two glycoside hydrolase family 26 (GH26) β-mannanases, BoMan26A and BoMan26B, and a GH36 α-galactosidase, BoGal36A. The PUL also includes two glycan-binding proteins, confirmed by β-mannan affinity electrophoresis. When this PUL was deleted, B. ovatus was no longer able to grow on locust bean galactomannan. BoMan26A primarily formed mannobiose from mannan polysaccharides. BoMan26B had higher activity on galactomannan with a high degree of galactosyl substitution and was shown to be endo-acting generating a more diverse mixture of oligosaccharides, including mannobiose. Of the two β-mannanases, only BoMan26B hydrolyzed galactoglucomannan. A crystal structure of BoMan26A revealed a similar structure to the exo-mannobiohydrolase CjMan26C from Cellvibrio japonicus, with a conserved glycone region (−1 and −2 subsites), including a conserved loop closing the active site beyond subsite −2. Analysis of cellular location by immunolabeling and fluorescence microscopy suggests that BoMan26B is surface-exposed and associated with the outer membrane, although BoMan26A and BoGal36A are likely periplasmic. In light of the cellular location and the biochemical properties of the two characterized β-mannanases, we propose a scheme of sequential action by the glycoside hydrolases encoded by the β-mannan PUL and involved in the β-mannan utilization pathway in B. ovatus. The outer membrane-associated BoMan26B initially acts on the polysaccharide galactomannan, producing comparably large oligosaccharide fragments. Galactomanno-oligosaccharides are further processed in the periplasm, degalactosylated by BoGal36A, and subsequently hydrolyzed into mainly mannobiose by the β-mannanase BoMan26A.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Galactomannan Catabolism Conferred by a Polysaccharide Utilization Locus of Bacteroides ovatus

Bågenholm

Reddy

Bouraoui

et al. 2017

Journal of Biological Chemistry

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156

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“…Furthermore, the adhesiveness of Neisseria gonorrhoeae to epithelial cells has been inhibited by the presence of cell surface enolase of a vaginal commensal bacterium, L. jensenii [39]. Moreover, enolase and GAPDH present in the extracellular proteome of L. crispatus ST1 and other commensal species has been shown to enhance tPA-mediated plasminogen activation [40].…”

Section: Moonlighting Functions Of Surface Layer Proteinsmentioning

confidence: 99%

Bacterial Surface Layer Proteins: From Moonlighting to Biomimetics: A New Horizonto Lead

Gaur¹,

Sharma²,

Singhal³

2018

ABB

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The landmark discovery of moonlighting proteins embarks the significant progress in understanding the biological complexity and their closed-circuit analysis. The growing continuum in the variety of moonlighting functions paved the way for further elucidation of structural-functional aspects of protein evolution and design of proteins with novel functions. Currently, the moonlighting functions in various adhesive properties of surface layer proteins, an essential component of cell surface architecture of archaea and all phylogenetic groups of eubacteria become more prominently recognized. The remarkable credentials of surface layer proteins to self-assemble into supramolecular structures at nano-scale dimension have been exploited for the production of smart biomaterials in the form of biomimetics has been thrust area of research. The finely tuned topological features in terms of shape, size, geometry and surface chemistry of surface layer proteins are crucial for the production of biomimetics. The current developments of biomimetic lipid bilayers and composite membranes find applicability in understanding the functional dynamism of evolutionary relationship of bacterial cell envelopes and vaccine development, drug development and drug delivery. Though the development of biomimetics embraces fascination but faces with technological challenges. The plethora of literature has been available for the moonlighting aspects and nano-technological applications separately but none of the review describes towards the rhythmic transition from moonlighting functions of surface layer proteins of bacteria to biomimetics development and applications. Therefore, this review describes certain basic aspects of moonlighting functions and their mechanism of action, surface layer proteins and their moonlighting functions of commensal bacteria and their transition towards biomimetics. The recent developments of biomimetics based on surface layer proteins have been summarized and also posited different chal-

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“…효소로는 곰팡이 유래 또는 세균 유래 효소가 두루 포함되어 있다 [10,11,23]. 최근에는 GH113에 속하는 Alicyclobacillus속 균주의 mannanase [19]와 GH134에 속하는 A. nidulans의 mannanase [13]가 보고되었다.…”

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Isolation of Mannanase-producing Bacteria, Bacillus subtilis WL-6 and WL-11, and Cloning and Characterization of Mannanase

Yoon¹

2016

Journal of Life Science

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Two bacterial strains producing extracellular man nanase were isolated from doenjang, a traditionally fermented soybean paste in Korea. The isolates, WL-6 and WL-11, were identified as Bacillus subtiis on the basis of their 16S rRNA gene sequences, morphological, and biochemical properties. Two genes encoding the mannanase of both B. subtilis WL-6 and B. subtilis WL-11 were each cloned into Escherichia coli, and their nucleotide sequences were determined. Both mannanase genes consisted of 1,086 nucleotides, encoding polypeptides of 362 amino acid residues. The deduced amino acid sequences of the two WL-6 and WL-11 mannanases, designated Man6 and Man11, respectively, differed from each other by eight amino acid residues, and they were highly homologous to those of mannanases belonging to the glycosyl hydrolase family 26. The 26 amino acid stretch in the N-terminus of Man6 and Man11 was a predicted signal peptide. Both Man6 and Man11 were localized at the level of 94-95% in an intracellular fraction of recombinant E. coli cells. The enzymes hydrolyzed both locust bean gum and mannooligosaccharides, including mannotriose, mannotetraose, mannopentaose, and mannohexaose, forming mannobiose and mannotriose as predominant products. The optimal reaction conditions were 55° C and pH 6.0 for Man6, and 60° C and pH 5.5 for Man11. Man11 was more stable than Man6 at high temperatures.

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The GH5 1,4-β-mannanase from Bifidobacterium animalis subsp. lactis Bl-04 possesses a low-affinity mannan-binding module and highlights the diversity of mannanolytic enzymes

Cited by 37 publications

References 59 publications

Galactomannan Catabolism Conferred by a Polysaccharide Utilization Locus of Bacteroides ovatus

Galactomannan Catabolism Conferred by a Polysaccharide Utilization Locus of Bacteroides ovatus

Bacterial Surface Layer Proteins: From Moonlighting to Biomimetics: A New Horizonto Lead

Isolation of Mannanase-producing Bacteria, Bacillus subtilis WL-6 and WL-11, and Cloning and Characterization of Mannanase

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