Characterization of a novel endo-levanase and its gene from Bacillus sp. L7

Miasnikov, Andrei N.

doi:10.1111/j.1574-6968.1997.tb12619.x

Cited by 21 publications

(7 citation statements)

References 14 publications

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“…Levanases (EC 3.2.1.65) are enzymes found in some microorganisms (e.g., Bacillus and Pseudomonas) that catalyze the hydrolysis of the β-2,6-linked main chain of levan, a natural product from the group of fructans (Murakami et al 1992; Miasnikov 1997). Levan polysaccharide is known to play an ecological role on Bacillus biofilm formation and maintenance (Marvasi et al 2010), while on some strains of Pseudomonas are suggested to be part of a protective capsule against phages (PATON 1960).…”

Section: Diversity Of Phage Depolymerasesmentioning

confidence: 99%

Bacteriophage-encoded depolymerases: their diversity and biotechnological applications

Pires

Oliveira

Melo

et al. 2016

Appl Microbiol Biotechnol

356

305

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Bacteriophages (phages), natural enemies of bacteria, can encode enzymes able to degrade polymeric substances. These substances can be found in the bacterial cell surface, such as polysaccharides, or are produced by bacteria when they are living in biofilm communities, the most common bacterial lifestyle. Consequently, phages with depolymerase activity have a facilitated access to the host receptors, by degrading the capsular polysaccharides, and are believed to have a better performance against bacterial biofilms, since the degradation of extracellular polymeric substances by depolymerases might facilitate the access of phages to the cells within different biofilm layers. Since the diversity of phage depolymerases is not yet fully explored, this is the first review gathering information about all the depolymerases encoded by fully sequenced phages. Overall, in this study, 160 putative depolymerases, including sialidases, levanases, xylosidases, dextranases, hyaluronidases, peptidases as well as pectate/pectin lyases, were found in 143 phages (43 Myoviridae, 47 Siphoviridae, 37 Podoviridae, and 16 unclassified) infecting 24 genera of bacteria. We further provide information about the main applications of phage depolymerases, which can comprise areas as diverse as medical, chemical, or food-processing industry.

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Section: Diversity Of Phage Depolymerasesmentioning

confidence: 99%

Bacteriophage-encoded depolymerases: their diversity and biotechnological applications

Pires

Oliveira

Melo

et al. 2016

Appl Microbiol Biotechnol

356

305

View full text Add to dashboard Cite

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“…In fact, this type of behavior is common to a number of polysaccharide hydrolases, which possess a single catalytic domain linked at either the N-or C-terminus to one or more polysaccharide (ligand) binding sites. 16 Contrary to LMW levan, most of the investigated levanases showed a negative cooperativity in the presence of the HMW levan substrate with Hill coefficients lower than 1. As indicated in Table 4, the maximum rate of levan hydrolysis (v max ) is highly differentiable among the levanases studied.…”

Section: Catalytic Properties Of Selected Levanase Candidatesmentioning

confidence: 98%

“…The last optimum temperature is higher than the other levanases we studied and those previously reported, with the exception of G. diazotrophicus SRT4 (45 °C), 15 Pseudomonas K-52 (70 °C), 22 and Bacillus sp. L7 (50 °C) 16 levanases. Indeed, Lim et al 9 reported 40 °C to be the optimal temperature for Streptomyces sp.…”

Section: Catalytic Properties Of Selected Levanase Candidatesmentioning

confidence: 99%

“…This is exemplified by levanases found in Bacillus subtilis , Actinomyces viscosus , Bacteroides fragilis, and Geobacillus stearothermophilus. − Some of these enzymes are not only capable of hydrolyzing levan, but also inulin, raffinose, and sucrose, although with different substrate specificities. Endo-levanases (EC 3.2.1.65) have been identified from Bacillus species, , Arthrobacter species, G. diazotrophicus SRT4, and Bacteriodes thetaiotaomicron.…”

Section: Introductionmentioning

confidence: 99%

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Discovery and Enzymatic Screening of Genome-Mined Microbial Levanases to Produce Second-Generation β-(2,6)-Fructooligosaccharides: Catalytic Properties

et al. 2023

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Evidence suggests that β-(2,6)-levan-type fructooligosaccharides (FOSs) possess higher prebiotic potential and selectivity than their β-(2,1)-inulin-type counterparts. The focus of the present work was to develop an enzymatic approach for the synthesis of levan-type FOSs, employing levanases (EC 3.2.1.65), specifically those performing endo-hydrolysis on levans. To identify new levanases, a selection of candidates was obtained via in silico exploration of the levanase family biodiversity through a sequence-driven approach. A collection of 113 candidates was screened according to their specific activities on low- and high-molecular-weight (MW) levan as well as thermal stability. The most active levanases were able to hydrolyze both types of levan with similar efficiency. This ultimately revealed 10 active, highly evolutionary distant and diverse candidate levanases, which demonstrated preferential hydrolysis of levan over inulin. The end-product profile differed significantly depending on levanase with levanbiose, levantriose, and levantetraose being the major FOSs. Among them, the catalytic properties of 5 selected potential new levanases (LEV9 from Belliella Baltica, LEV36 from Dyadobacter fermentans, LEV37 from Capnocytophaga ochracea, LEV79 from Vibrio natriegens, LEV91 from Paenarthrobacter aurescens) were characterized, especially in terms of pH and temperature profiles, thermal stability, and kinetic parameters. The identification of these novel levanases is expected to contribute to the production of levan-type FOSs with properties surpassing those of commercial preparations.

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“…PSDs collectively have a broad diversity in terms of their substrate specificities [ 18 ], although they can be generally differentiated into two classes: hydrolases and lyases [ 85 ] ( Figure 4 ). The hydrolases catalyze the hydrolysis of glycosidic bonds [ 58 ] and currently include six groups: sialidases (hydrolyzing α-2,8-linkages in capsular polysialic acid) [ 86 ], rhamnosidases (cleaving α-1,3 O-glycosidic bonds between L-rhamnose and D-galactose) [ 87 ], levanases (hydrolyzing β-2,6-bonds between fructose monomers in levan) [ 88 , 89 ], xylanases (cutting β-1,4 bonds within xylan) [ 90 , 91 , 92 , 93 ], dextranases (cleaving α-1,6-linkages between glucose units in dextran) [ 94 , 95 ], and LPS deacetylases (deacetylating the O-antigen) [ 55 , 66 , 96 ]. The lyases instead cleave (1,4) glycosidic bonds by a β-elimination mechanism [ 97 , 98 ] and currently comprise five groups: hyaluronate lyase (cleaving β-1,4 bonds in hyaluronic acid) [ 99 ], pectate lyase (cleaving α-1,4 bonds of polygalacturonic acid) [ 100 , 101 ], alginate lyase (cutting α-1,4 bonds of alginate) [ 102 , 103 ], K5 lyase (cleaving α-1,4 bonds of E. coli K5 capsules) [ 104 ], and O-specific polysaccharide lyase (cleaving of O-specific antigen of LPS) [ 105 ].…”

Section: Phage-encoded Polysaccharide Depolymerases (Psds)mentioning

confidence: 99%

Treating Bacterial Infections with Bacteriophage-Based Enzybiotics: In Vitro, In Vivo and Clinical Application

2021

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Over the past few decades, we have witnessed a surge around the world in the emergence of antibiotic-resistant bacteria. This global health threat arose mainly due to the overuse and misuse of antibiotics as well as a relative lack of new drug classes in development pipelines. Innovative antibacterial therapeutics and strategies are, therefore, in grave need. For the last twenty years, antimicrobial enzymes encoded by bacteriophages, viruses that can lyse and kill bacteria, have gained tremendous interest. There are two classes of these phage-derived enzymes, referred to also as enzybiotics: peptidoglycan hydrolases (lysins), which degrade the bacterial peptidoglycan layer, and polysaccharide depolymerases, which target extracellular or surface polysaccharides, i.e., bacterial capsules, slime layers, biofilm matrix, or lipopolysaccharides. Their features include distinctive modes of action, high efficiency, pathogen specificity, diversity in structure and activity, low possibility of bacterial resistance development, and no observed cross-resistance with currently used antibiotics. Additionally, and unlike antibiotics, enzybiotics can target metabolically inactive persister cells. These phage-derived enzymes have been tested in various animal models to combat both Gram-positive and Gram-negative bacteria, and in recent years peptidoglycan hydrolases have entered clinical trials. Here, we review the testing and clinical use of these enzymes.

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Characterization of a novel endo-levanase and its gene from Bacillus sp. L7

Cited by 21 publications

References 14 publications

Bacteriophage-encoded depolymerases: their diversity and biotechnological applications

Bacteriophage-encoded depolymerases: their diversity and biotechnological applications

Discovery and Enzymatic Screening of Genome-Mined Microbial Levanases to Produce Second-Generation β-(2,6)-Fructooligosaccharides: Catalytic Properties

Treating Bacterial Infections with Bacteriophage-Based Enzybiotics: In Vitro, In Vivo and Clinical Application

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