The amino acid sequences of 301 glycosyl hydrolases and related enzymes have been compared. A total of 291 sequences corresponding to 39 EC entries could be classified into 35 families. Only ten sequences (less than 5% of the sample) could not be assigned to any family. With the sequences available for this analysis, 18 families were found to be monospecific (containing only one EC number) and 17 were found to be polyspecific (containing at least two EC numbers). Implications on the folding characteristics and mechanism of action of these enzymes and on the evolution of carbohydrate metabolism are discussed. With the steady increase in sequence and structural data, it is suggested that the enzyme classification system should perhaps be revised.

A classification of glycosyl hydrolases based on amino acid sequence similarities.

Pathogenic microorganisms affecting plant health are a major and chronic threat to food production and ecosystem stability worldwide As agricultural production intensified over the past few decades, producers became more and more dependent on agrochemicals as a relatively reliable method of crop

Use of Plant Growth-Promoting Bacteria for Biocontrol of Plant Diseases: Principles, Mechanisms of Action, and Future Prospects

The worldwide increases in both environmental damage and human population pressure have the unfortunate consequence that global food production may soon become insufficient to feed all of the world's people. It is therefore essential that agricultural productivity be significantly increased within the next few decades. To this end, agricultural practice is moving toward a more sustainable and environmentally friendly approach. This includes both the increasing use of transgenic plants and plant growth-promoting bacteria as a part of mainstream agricultural practice. Here, a number of the mechanisms utilized by plant growth-promoting bacteria are discussed and considered. It is envisioned that in the not too distant future, plant growth-promoting bacteria (PGPB) will begin to replace the use of chemicals in agriculture, horticulture, silviculture, and environmental cleanup strategies. While there may not be one simple strategy that can effectively promote the growth of all plants under all conditions, some of the strategies that are discussed already show great promise.

/pdf/plant-growth-promoting-bacteria-mechanisms-and-applications-1vmnc8frke.pdf

Plant Growth-Promoting Bacteria: Mechanisms and Applications

Acetone-butanol fermentation revisited.

https://www.sbmicrobiologia.org.br/PDF/4.pdf

Bio-hydrogen production from waste materials

The effect of pH, growth rate, phosphate and iron limitation, carbon monoxide, and carbon source on product formation by Clostridium pasteurianum was determined. Under phosphate limitation, glucose was fermented almost exclusively to acetate and butyrate independently of the pH and growth rate. Iron limitation caused lactate production (38 mol/100 mol) from glucose in batch and continuous culture. At 15% (vol/vol) carbon monoxide in the atmosphere, glucose was fermented to ethanol (24 mol/100 mol), lactate (32 mol/100 mol), and butanol (36 mol/100 mol) in addition to the usual products, acetate (38 mol/100 mol) and butyrate (17 mol/100 mol). During glycerol fermentation, a completely different product pattern was found. In continuous culture under phosphate limitation, acetate and butyrate were produced only in trace amounts, whereas ethanol (30 mol/100 mol), butanol (18 mol/100 mol), and 1,3-propanediol (18 mol/100 mol) were the major products. Under iron limitation, the ratio of these products could be changed in favor of 1,3-propanediol (34 mol/100 mol). In addition, lactate was produced in significant amounts (25 mol/100 mol). The tolerance of C. pasteurianum to glycerol was remarkably high; growth was not inhibited by glycerol concentrations up to 17% (wt/vol). Increasing glycerol concentrations favored the production of 1,3-propanediol.

Parameters Affecting Solvent Production by Clostridium pasteurianum.

Metabolic engineering of Clostridium acetobutylicum: recent advances to improve butanol production

Clostridium acetobutylicum cells were collected from chemostats which were run at pH 4.3 or 6.0 and which produced either acetone-butanol or acetate-butyrate; they were used to determine the level of enzymes involved either in solvent or in acid formation. The highest activity of phosphotransacetylase, phosphotransbutyrylase, acetate kinase, and butyrate kinase was found in cells which carried out an acetate-butyrate fermentation; these enzymes were present in solvent-producing cells at a level of about 10–50% as compared to acid-producing cells. Hydrogenase activity was detectable in approximately the same amounts in both cell types; however, in solvent-producing cells it was only measurable following a lag-period. Butyraldehyde and butanol dehydrogenases were found in small amounts exclusively in solvent-producing cells. It was demonstrated that the formation of acetone was initiated by the action of a coenzyme A-transferase which transferred coenzyme A from acetoacetyl-CoA to either acetate or butyrate. This coenzyme A-transferase as well as acetoacetate decarboxylase were hardly detectable in acid-producing cells, but reached high levels in solvent producing cells. Similar changes of the activity of the enzymes mentioned were observed when a batch culture was shifted from acid to solvent formation.

Level of enzymes involved in acetate, butyrate, acetone and butanol formation by Clostridium acetobutylicum

When Clostridium acetobutylicum was grown in continuous culture under glucose limitation at neutral pH and varying dilution rates the only fermentation products formed were acetate, butyrate, carbon dioxide and molecular hydrogen. The Y
 glucose
 max
 and (Y
 ATP
 max
 )
 gluc
 exp
 values were 48.3 and 23.8 dry weight/mol, respectively. Acetone and butanol were produced when the pH was decreased below 5.0 (optimum at pH 4.3). The addition of butyric acid (20 to 80 mM) to the medium with a pH of 4.3 resulted in a shift of the fermentation from acid, to solvent formation.

Effect of pH and butyrate concentration on the production of acetone and butanol by Clostridium acetobutylicum grown in continuous culture

The chitinolytic rhizobacterium Serratia plymuthica HRO-C48 was previously selected as a biocontrol agent of phytopathogenic fungi. One endochitinase (E.C. 3.2.1.14), CHIT60, and one N-acetyl-β-1,4-D-hexosaminidase (E.C. 3.2.1.52), CHIT100, were purified and characterized. The endochitinase CHIT60, with an apparent molecular mass of 60.5 kDa, had a N-terminal amino acid sequence highly similar to that of chitinases A from Serratia liquefaciens and Serratia marcescens. The enzyme activity had its peak at 55 °C and pH 5.4, and increased by more than 20% in the presence of 10 mM Ca2+, Co2+ or Mn2+. Activity was inhibited by 80% in the presence of 10 mM Cu2+. CHIT100 appeared to be a monomeric enzyme with a molecular mass of 95.6 kDa and a pI of 6.8. Optimal activity was obtained at 43 °C and pH 6.6, and decreased by more than 90 % in the presence of 10 mM Co2+ or Cu2+. CHIT100 (100 µg ml–1) inhibited spore germination and germ tube elongation of the phytopathogenic fungus Botrytis cinerea by 28 % and 31.6 %, respectively. With CHIT60 (100 µg ml–1), the effect was more pronounced: 78 % inhibition of of germination and 63.9 % inhibition of germ tube elongation.

Hubert Bahl

Papers

Parameters Affecting Solvent Production by Clostridium pasteurianum.

Metabolic engineering of Clostridium acetobutylicum: recent advances to improve butanol production

Level of enzymes involved in acetate, butyrate, acetone and butanol formation by Clostridium acetobutylicum

Effect of pH and butyrate concentration on the production of acetone and butanol by Clostridium acetobutylicum grown in continuous culture

Purification and properties of two chitinolytic enzymes of Serratia plymuthica HRO-C48