Cell Wall Biomass Research Articles

X-ray Crystal Structure of a Non-crystalline Cellulose-specific Carbohydrate-binding Module: CBM28

Natural cellulose exists as a composite of different forms, which have historically been broadly characterized as “crystalline” or “amorphous”. The recognition of both of these forms of cellulose by the carbohydrate-binding modules (CBM) of microbial glycoside hydrolases is central to natural and efficient biotechnological conversion of plant cell wall biomass. There is increasing evidence that, at least some, individual binding modules target distinct and different regions of non-crystalline “amorphous” cellulose. Competition experiments show that CBM28 modules do not compete with CBM17 modules when binding to non-crystalline cellulose. The structure of the BspCBM28 (http://afmb.cnrs-mrs.fr/CAZY/) module from the Bacillus sp. 1139 family GH5 endoglucanase, comprising a 191 amino acid protein, has therefore been determined at 1.4 Å resolution using single isomorphous replacement with anomalous scattering methods. The structure reveals a “β-jelly roll” topology, with high degree of similarity to the structure of CBM17 domains. Sequence and structural conservation strongly suggests that these two families of domains have evolved through gene duplication and subsequent divergence. The ligand-binding site “topographies” of CBMs from families 28, 17 and 4 begins to shed light on the differential recognition of non-crystalline cellulose by multi-modular plant cell wall-degrading enzymes.

X-ray Crystal Structure of a Non-crystalline Cellulose-specific Carbohydrate-binding Module: CBM28

Natural cellulose exists as a composite of different forms, which have historically been broadly characterized as “crystalline” or “amorphous”. The recognition of both of these forms of cellulose by the carbohydrate-binding modules (CBM) of microbial glycoside hydrolases is central to natural and efficient biotechnological conversion of plant cell wall biomass. There is increasing evidence that, at least some, individual binding modules target distinct and different regions of non-crystalline “amorphous” cellulose. Competition experiments show that CBM28 modules do not compete with CBM17 modules when binding to non-crystalline cellulose. The structure of the BspCBM28 ( http://afmb.cnrs-mrs.fr/CAZY/) module from the Bacillus sp. 1139 family GH5 endoglucanase, comprising a 191 amino acid protein, has therefore been determined at 1.4 Å resolution using single isomorphous replacement with anomalous scattering methods. The structure reveals a “β-jelly roll” topology, with high degree of similarity to the structure of CBM17 domains. Sequence and structural conservation strongly suggests that these two families of domains have evolved through gene duplication and subsequent divergence. The ligand-binding site “topographies” of CBMs from families 28, 17 and 4 begins to shed light on the differential recognition of non-crystalline cellulose by multi-modular plant cell wall-degrading enzymes.

Adsorption and reduction of palladium (Pd2+) by Bacillus licheniformis R08

Preliminary study on the mechanism of Pd2+ biosorption by resting cells of Bacillus licheniformis R08 biomass has been carried out by means of chemical kinetics and AAS, TEM, XRD and FTIR methods. The results showed that at 30°C and pH 3.5, when dry R08 biomass powder (800 mg/L) was mixed with Pd2+ (100 mg/L) for 45 min, the rate constant k of biosorption of Pd2+ attained a maximum of 5.97 × 10−2 min−1 and the half life period of the reaction reached 12 min. The part of Pd2+ adsorbed by R08 biomass was reduced to elemental, cell-bound Pd at the same condition. The cell wall of R08 biomass was the primary location for accumulating Pd2+, and aldoses, i. e. hydrolysate of a part of polysaccharides on the peptidoglycan layer in the acidic medium, serving as the electron donor, in situ reduced the Pd2+ to Pd0.

Biosorption of heavy metals by Sphaerotilus natans: an equilibrium study at different pH and biomass concentrations

In the present work a lyophilised cell suspension of Spherotilus natans was studied as biosorbent material for cadmium and copper removal from aqueous solutions. The biomass was firstly characterised by potentiometric titration and evaluation of the major ionic content. The experimental data highlight that the biomass cell wall contains two main acidic groups with a total amount of 5 meq/g. Equilibrium biosorption trials of cadmium and copper were carried out to investigate the effects of two important experimental factors, pH and biomass concentration. As expected, both cadmium and copper biosorption extent was repressed by pH decrease. The effect of the biomass concentration changes both with the equilibrium pH value and the kind of metal adsorbed. In the case of copper biosorption at pH>5, the increase of biomass concentration causes a diminution of the maximum specific metal uptake due probably to cell aggregation phenomena; whereas at acidic pH values the previous trend is inverted perhaps because of the effect of partial hydrolysis of the bacterial cell wall constituents. A different behaviour was observed for cadmium biosorption in relation to the microbial cell concentration: the effect of biomass concentration is less evident and opposite with respect to copper at pH 6 and 3 and no definitive explanation was found for this case. Equilibrium modelling was performed for both metals by using the most used equations reported in the literature. A comparison of the biosorption characteristic of S. natans has been also performed with respect to some results reported by other researchers.

Binding Mechanism of Heavy Metals Biosorption by Pycnoporus Sanguineus

Non-living biomass of Pycnoporus sanguineus has an ability to take up lead,copper and cadmium ions from an aqueous solution. The role played by various functional groups in the cell wall and the mechanism uptake of lead, copper and cadmium by Pycnoporus sanguineus were investigated. Modification of the functional groups such as lipids, carboxylic and amino was done through chemical pretreatment in order to study their role in biosorption of metal ions. Results showed that the chemical modification of these functional groups has modified the ability of biomass to remove lead, copper and cadmium ions from the solution. Scanning electron microscopy was also used to study the morphological structure of the biomass before and after adsorption. The electron micrograph indicated that the structure of biomass changed due to the adsorption of the metals onto the cell walls. Furthermore, the X-ray energy dispersion analysis (EDAX) showed that the calcium ion present in the cell wall of biomass was released and replaced by lead ions. This implied that an ion exchange is one of the principal mechanisms for metal biosorption.

A method to increase silver biosorption by an industrial strain of Saccharomyces cerevisiae.

Ag+ biosorption by an industrial strain of Saccharomyces cerevisiae was investigated. Older (96 h old) biomass had half the biosorption capacity of younger (24 h old) biomass (0.187 and 0.387 mmol Ag+/g dry mass respectively). Comparisons of cell walls isolated from biomass of either age indicated that chemical composition and Ag+ biosorption capacity varied little over the time span examined and that cell walls from either age of culture had small Ag+ biosorption capacities compared to whole cells of a similar age. Silver-containing precipitates were observed both on the cell wall and within the cell, indicating that intracellular components sorbed Ag+. The concentration of these precipitates within the cell appeared visually to decrease with age in Ag(+)-exposed cells. Incorporation of L-cysteine into the growth medium resulted in biomass with increased silver biosorption capacities, protein and sulphydryl group content. Increasing the concentration of L-cysteine in the growth medium from 0 to 5.0 mM increased silver biosorption from 0.389 to 0.556 mmol Ag+/g dry mass. Isolated cell walls of biomass grown in supplemented media also showed a possible link between silver biosorption capacities, protein and sulphydryl group content. No precipitates were observed in silver-exposed biomass that had been grown in the presence of 5.0 mM L-cysteine.