scholarly journals Green Production and Biotechnological Applications of Cell Wall Lytic Enzymes

2019 ◽  
Vol 9 (23) ◽  
pp. 5012 ◽  
Author(s):  
Benedetti ◽  
Locci ◽  
Gramegna ◽  
Sestili ◽  
Savatin

: Energy demand is constantly growing, and, nowadays, fossil fuels still play a dominant role in global energy production, despite their negative effects on air pollution and the emission of greenhouse gases, which are the main contributors to global warming. An alternative clean source of energy is represented by the lignocellulose fraction of plant cell walls, the most abundant carbon source on Earth. To obtain biofuels, lignocellulose must be efficiently converted into fermentable sugars. In this regard, the exploitation of cell wall lytic enzymes (CWLEs) produced by lignocellulolytic fungi and bacteria may be considered as an eco-friendly alternative. These organisms evolved to produce a variety of highly specific CWLEs, even if in low amounts. For an industrial use, both the identification of novel CWLEs and the optimization of sustainable CWLE-expressing biofactories are crucial. In this review, we focus on recently reported advances in the heterologous expression of CWLEs from microbial and plant expression systems as well as some of their industrial applications, including the production of biofuels from agricultural feedstock and of value-added compounds from waste materials. Moreover, since heterologous expression of CWLEs may be toxic to plant hosts, genetic strategies aimed in converting such a deleterious effect into a beneficial trait are discussed.

1993 ◽  
pp. 253-259
Author(s):  
Rubens López ◽  
José L. García ◽  
Eduardo Díaz ◽  
Jesús M. Sanz ◽  
José M. Sánchez-Puelles ◽  
...  

2020 ◽  
Vol 295 (27) ◽  
pp. 9171-9182 ◽  
Author(s):  
Danielle L. Sexton ◽  
Francesca A. Herlihey ◽  
Ashley S. Brott ◽  
David A. Crisante ◽  
Evan Shepherdson ◽  
...  

Bacterial dormancy can take many forms, including formation of Bacillus endospores, Streptomyces exospores, and metabolically latent Mycobacterium cells. In the actinobacteria, including the streptomycetes and mycobacteria, the rapid resuscitation from a dormant state requires the activities of a family of cell-wall lytic enzymes called resuscitation-promoting factors (Rpfs). Whether Rpf activity promotes resuscitation by generating peptidoglycan fragments (muropeptides) that function as signaling molecules for spore germination or by simply remodeling the dormant cell wall has been the subject of much debate. Here, to address this question, we used mutagenesis and peptidoglycan binding and cleavage assays to first gain broader insight into the biochemical function of diverse Rpf enzymes. We show that their LysM and LytM domains enhance Rpf enzyme activity; their LytM domain and, in some cases their LysM domain, also promoted peptidoglycan binding. We further demonstrate that the Rpfs function as endo-acting lytic transglycosylases, cleaving within the peptidoglycan backbone. We also found that unlike in other systems, Rpf activity in the streptomycetes is not correlated with peptidoglycan-responsive Ser/Thr kinases for cell signaling, and the germination of rpf mutant strains could not be stimulated by the addition of known germinants. Collectively, these results suggest that in Streptomyces, Rpfs have a structural rather than signaling function during spore germination, and that in the actinobacteria, any signaling function associated with spore resuscitation requires the activity of additional yet to be identified enzymes.


1966 ◽  
Vol 30 (11) ◽  
pp. 1097-1101
Author(s):  
Kenji Sakaguchi ◽  
Shozo Kotani ◽  
Hidekazu Suginaka ◽  
Yoshiyuki Hirachi ◽  
Shuzo Kashiba ◽  
...  

2008 ◽  
Vol 74 (24) ◽  
pp. 7490-7496 ◽  
Author(s):  
Yu Pei Tan ◽  
Philip M. Giffard ◽  
Daniel G. Barry ◽  
Wilhelmina M. Huston ◽  
Mark S. Turner

ABSTRACT Lactococcus lactis is a gram-positive bacterium that is widely used in the food industry and is therefore desirable as a candidate for the production and secretion of recombinant proteins. Previously, we generated a L. lactis strain that expressed and secreted the antimicrobial cell wall-lytic enzyme lysostaphin. To identify lactococcal gene products that affect the production of lysostaphin, we isolated and characterized mutants generated by random transposon mutagenesis that had altered lysostaphin activity. Out of 35,000 mutants screened, only one with no lysostaphin activity was identified, and it was found to contain an insertion in the lysostaphin expression cassette. Ten mutants with higher lysostaphin activity contained insertions in only four different genes, which encode an uncharacterized putative transmembrane protein (llmg_0609) (three mutants), an enzyme catalyzing the first step in peptidoglycan biosynthesis (murA2) (five mutants), a putative regulator of peptidoglycan modification (trmA) (one mutant), and an uncharacterized enzyme possibly involved in ubiquinone biosynthesis (llmg_2148) (one mutant). These mutants were found to secrete larger amounts of lysostaphin than the control strain (MG1363[lss]), and the greatest increase in secretion was 9.8- to 16.1-fold, for the llmg_0609 mutants. The lysostaphin-oversecreting llmg_0609, murA2, and trmA mutants were also found to secrete larger amounts of another cell wall-lytic enzyme (the Listeria monocytogenes bacteriophage endolysin Ply511) than the control strain, indicating that the phenotype is not limited to lysostaphin.


1966 ◽  
Vol 30 (11) ◽  
pp. 1097-1101
Author(s):  
Kenji SAKAGUCHI ◽  
Shozo KOTANI ◽  
Hidekazu SUGINAKA ◽  
Yoshiyuki HIRACHI ◽  
Shuzo KASHIBA ◽  
...  

Nature ◽  
1966 ◽  
Vol 210 (5034) ◽  
pp. 442-443 ◽  
Author(s):  
MARIA VICTORIA ELORZA ◽  
E. MUÑOZ RUIZ ◽  
JULIO R. VILLANUEVA

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