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Review
. 2021 Aug 3;30(10):1277-1291.
doi: 10.1007/s10068-021-00957-1. eCollection 2021 Oct.

Potential applications of recombinant bifidobacterial proteins in the food industry, biomedicine, process innovation and glycobiology

José A Morales-Contreras  1 , Jessica E Rodríguez-Pérez  1 , Carlos A Álvarez-González  2 , Mirian C Martínez-López  1 , Isela E Juárez-Rojop  1   2 , Ángela Ávila-Fernández  1
Affiliations
Review

Potential applications of recombinant bifidobacterial proteins in the food industry, biomedicine, process innovation and glycobiology

José A Morales-Contreras et al. Food Sci Biotechnol. .

Abstract

Bifidobacterial proteins have been widely studied to elucidate the metabolic mechanisms of diet adaptation and survival of Bifidobacteria, among others. The use of heterologous expression systems to obtain proteins in sufficient quantities to be characterized has been essential in these studies. L. lactis and the same Bifidobacterium as expression systems highlight ways to corroborate some of the functions attributed to these proteins. The most studied proteins are enzymes related to carbohydrate metabolism, particularly glycosidases, due to their potential application in the synthesis of neoglycoconjugates, prebiotic neooligosaccharides, and active metabolites as well as their high specificity and efficiency in processing glycoconjugates. In this review, we classified the recombinant bifidobacterial proteins reported to date whose characterization has demonstrated their usefulness or their ability to produce a product of commercial interest for the food industry, biomedicine, process innovation and glycobiology. Future directions for their study are also discussed.

Supplementary information: The online version contains supplementary material available at 10.1007/s10068-021-00957-1.

Keywords: Bifidobacteria; Expression systems; Probiotic; Recombinant proteins.

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Conflict of interest statement

Conflict of interestThe authors declare that there is no conflict of interest.

Figures

Fig. 1
Fig. 1
Heterologous expression systems used to produce bifidobacterial recombinant proteins
Fig. 2
Fig. 2
Enzymatic activities and functions of recombinant bifidobacterial proteins used in the food industry (A), biomedicine (B), innovation of industrial processes (C), and glycobiology (D). Each symbol represents a specific monosaccharide found in nature according to Symbol Nomenclature for Graphical Representation of Glycans (Varki et al., 2015). AgnB (α-N-acetylglucosaminidase), aRham (α-L-rhamnosidase), BbAfcA N423H (1,2-α-L-fucosyntase), BbBgI (β-glucosidase), BbhI (β-N-acetylhexosaminidase), b-Gal (β-galactosidase), BiLA (α-amylase), BiUSP or BLUSP (UDP-sugar pyrophosphorylase), BtAS (amylosucrase), EndoBI (endo-β-N-acetylglucosaminidase), EngBF (endo-α-N-acetylgalactosaminidase), ESBP (extracelular solute-binding protein), GalE (UDP-glucose epimerase), GalT (UDP-glucose-hexose-1-phosphate uridylyltransferase), HypBA2 (β-L-arabinobiosidase), L-AI (L-arabinose isomerase), LNBase (lacto-N-biosidase), NagBb (exo/endo-α-N-acetylgalactosaminidase), NahK_ATCC15697 (N-acetylhexosamine 1-kinase), SP (sucrose phosphorylase)
See this image and copyright information in PMC

References

    1. Arreola SL, Intanon M, Suljic J, Kittl R, Pham NH, Kosma P, Haltrich D, Nguyen T-H. Two β-galactosidases from the human isolate Bifidobacterium breve DSM 20213: Molecular cloning and expression, biochemical characterization and synthesis of galacto-oligosaccharides. PLoS ONE. 2014;9:e104056. doi: 10.1371/journal.pone.0104056. - DOI - PMC - PubMed
    1. Ashida H, Miyake A, Kiyohara M, Wada J, Yoshida E, Kumagai H, Katayama T, Yamamoto K. Two distinct α-L-fucosidases from Bifidobacterium bifidum are essential for the utilization of fucosylated milk oligosaccharides and glycoconjugates. Glycobiology. 2009;19(9):1010–1017. doi: 10.1093/glycob/cwp082. - DOI - PubMed
    1. Ashida H, Ozawa H, Fujita K, Suzuki S, Yamamoto K. Syntheses of mucin-type O-glycopeptides and oligosaccharides using transglycosylation and reverse-hydrolysis activities of Bifidobacterium endo-α-N-acetylgalactosaminidase. Glycoconjugate Journal. 2010;27(1):125–132. doi: 10.1007/s10719-009-9247-8. - DOI - PubMed
    1. Assenberg R, Wan PT, Geisse S, Mayr LM. Advances in recombinant protein expression for use in pharmaceutical research. Current Opinion in Structural Biology. 2013;23:393–402. doi: 10.1016/j.sbi.2013.03.008. - DOI - PubMed
    1. Ávila-Fernández A, Cuevas-Juárez E, Rodríguez-Alegría ME, Olvera C, López-Munguía A. Functional characterization of a novel β-fructofuranosidase from Bifidobacterium longum subsp. infantis ATCC 15697 on structurally diverse fructans. Journal of Applied Microbiology. 2016;121:263–276. doi: 10.1111/jam.13154. - DOI - PubMed

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