The role of conserved non-aromatic residues in the Lactobacillus amylovorus α-amylase CBM26-starch interaction

Armenta, Silvia; Sánchez-Cuapio, Zaira; Munguı́a, Maria Elena; Pulido, Nancy O.; Farrés, Amelia; Manoutcharian, Karen; Hernández-Santoyo, Alejandra; Moreno-Mendieta, Silvia; Sánchez, Sergio; Rodríguez‐Sanoja, Romina

doi:10.1016/j.ijbiomac.2018.10.061

Cited by 9 publications

(8 citation statements)

References 50 publications

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“…The presence of Lactobacillus oligofermentans and Lactobacillus sp . in diet 3 based on digestion of TPS/PLA film, confirm that are bacteria part of the obligate heterofermentative lactobacilli, which degrade carbohydrates only through the phosphoketolase via (Felis & Dellaglio, 2007), some authors report that Lactobacillus have some enzymatic properties to convert starch into lactic acid due to α‐amylase (Giraud et al., 1991), which is considered as amylolytic lactic acid bacteria (Armenta et al., 2019; Narita et al., 2006; Okafor et al., 1984; Scheirlinck et al., 1989), this possibly indicates deterioration and possible assimilation of carbohydrates in Coleoptera intestine, and can degrade the thermoplastic starch present in the film by enzymatic glucosylation (Wang et al., 2019), they also have ß‐galactosidase, an enzyme that hydrolyses lactose (Gheytanchi et al., 2010), and can degrade the lactic acid chains of the polymer, by it transglycosylation and transgalactosylation properties (Sheik & Gunasekaran, 2010). Lactobacillus oligofermentans is associated with deterioration of poultry products packaged in modified atmosphere (Koort et al., 2005), and is a Gram‐positive bacterium related to deterioration of meat products due to rigour mortis processes and production of acetic acid, by hydrolysis production of polylactic acid to lactic acid and then smaller monomers.…”

Section: Resultsmentioning

confidence: 96%

Intestinal microbiome changes of Ulomoides dermestoides (Chevrolat, 1878) fed with a film based on thermoplastic cassava starch and polylactic acid

Salazar‐Sánchez

Herrera

Flores‐Gallegos

et al. 2022

Environmental Quality Mgmt

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Degradation of polymers by insects is investigated because these materials are source of pollution. The objective of this study was to determine changes in the intestinal microbiome of Coleoptera Ulomoides dermestoides subjected to three polymeric diets based on oats (1), thermoplastic cassava starch (TPS) (2), and an extruded matrix (3) composed of TPS and polylactic acid (PLA). Insects were identified by sequencing of CO1, while gut microflora from insects was identified using DGGE and DNA sequencing. The intestinal microbiota of insects fed diet 1 was composed by Enterobacter sp., Enterococcus durans, Enterococcus faecalis, Escherichia sp., and Pantoea vagans, diet 2 by Bacillus maritimus, Enterobacter sp. non-culturable, Enterococcus alcedines, Lactobacillus oeni, Enterococcus faecalis and Escherichia sp., while diet 3 by Enterobacter sp., Enterococcus aquimarinus, Enterococcus casseliflavus, Enterococcus faecalis, Escherichia sp., and Lactobacillus oligofermentans indicating that the mixture of renewable sources present in the polymer such as TPS/PLA has a higher rate of degradation and assimilation and more diversity in the intestinal microbiome of insects than in the monopolymeric diets such as 1 and 2, and it was evidenced that diet changes the microbiome of the digestive tract of U. dermestoides which can be used during biodegradation of polymers.

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Section: Resultsmentioning

confidence: 96%

Intestinal microbiome changes of Ulomoides dermestoides (Chevrolat, 1878) fed with a film based on thermoplastic cassava starch and polylactic acid

Salazar‐Sánchez

Herrera

Flores‐Gallegos

et al. 2022

Environmental Quality Mgmt

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“…The quantitative binding capacity of the wild-type La CBM26 and derived mutated proteins was determined by ITC using an ITC 200 (Malvern) in 50 mM citrate-phosphate pH 5.5 at 25 °C as described in [1] . The data show no interaction between the protein and the carbohydrate; thus, no data analysis was done.…”

Section: Experimental Design Materials and Methodsmentioning

confidence: 99%

“…CD spectroscopy was carried out at 20 °C on a J-710 spectropolarimeter (Jasco Inc., Easton, MD, USA) with purified proteins as described in [1] . The effect of the addition of the ligand on the secondary structure was checked by adding to La CBM26 13 µM, β-cyclodextrin to a final concentration of 39 µM.…”

Section: Experimental Design Materials and Methodsmentioning

confidence: 99%

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Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26

et al. 2018

Self Cite

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Carbohydrate-binding modules (CBMs) are auxiliary domains into glycoside-hydrolases that allow the interaction between the insoluble substrate and the solubilized enzyme, through hydrophobic, CH-π interactions and hydrogen bonds. Here, we present the data article related to the interaction of one LaCBM26 and some mutated proteins with soluble α-glucans determined by enzyme-linked carbohydrate-binding assay, isothermal titration calorimetry (ITC), and affinity gel electrophoresis (AGE). The data of the behavior of proteins in presence and absence of substrate analyzed by circular dichroism CD and thermofluor are also presented. These results are complementary to the research article “The role of conserved non-aromatic residues in the Lactobacillus amylovorus α-amylase CBM26-starch interaction” (Armenta et al., 2019).

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“…3.2.1. Glycosyl Hydrolases 3.2.1.1. alpha-Amylase (Lactobacillus amylovorus NRRL B-4540 and other strains, L. plantarum, L. manihotiovorans); CBM26 (starch-binding) [3], [27], [33]. alpha-Amylase Amy13K (Eubacterium rectale); five CBM: different specificities [11].…”

Section: Probiotic Lectinsmentioning

confidence: 99%

Enzybiotics with Lectin Properties and Lectinbiotics with Enzyme Activities – Multifunctional Modulators of Communications in Organism: Fundamentals and Unlimited Potential in Food Industry, Biosensors and Medicine

Lakhtin

Davydkin

et al. 2021

EJBIO

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Examples of the nomenclature enzymes of all known classes with intrinsic lectin properties are represented, described and ordered. Such bi/multifunctional enzymes (enzybiotics) act as communicative agents, possess independent carbohydrate binding motifs, domains, epitopes or modules within subunit/molecule or supra-molecular assembly (free or solid-phased). Lectin part serve as modulator, switch and/or navigator of the whole resulting pattern enzyme (involving both catalytic center and lectinic sites) specificities toward targets. These enzybiotics (native and recombinant) as well as lectinbiotics (lectin-biotics) with intrinsic enzyme activities and high communicative potential possess promising broad prospects in food industry, medical biotechnology, prophylaxis and therapy. Among examples there are probiotic lectin enzybiotics (mainly from bifidobacteria and lactobacilli) that can serve perspective metabolite postbiotic systems for support or correction of the healthy individual or the patient mucosal open cavity biotope pathological status, respectively. Lectin-enzyme relationships improve platform for constructing advanced autoregulated systems influencing interactome at all levels of the organism. They support a lot of possible innovations in industrial biotechnology and medicine.

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The role of conserved non-aromatic residues in the Lactobacillus amylovorus α-amylase CBM26-starch interaction

Cited by 9 publications

References 50 publications

Intestinal microbiome changes of Ulomoides dermestoides (Chevrolat, 1878) fed with a film based on thermoplastic cassava starch and polylactic acid

Intestinal microbiome changes of Ulomoides dermestoides (Chevrolat, 1878) fed with a film based on thermoplastic cassava starch and polylactic acid

Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26

Enzybiotics with Lectin Properties and Lectinbiotics with Enzyme Activities – Multifunctional Modulators of Communications in Organism: Fundamentals and Unlimited Potential in Food Industry, Biosensors and Medicine

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