Acrylamide,a potential human carcinogen,formed in Maillard reaction model system was analyzed through pyrolysis-GC/MS.The study revealed that de-carboxylated schiff base and dicarbonyl compounds,such as pyruvic aldehyde,diacetyl,glyoxal,played important roles in acrylamide formation via a browning reaction,and comfirmed some key mediates in the formation of acrylamide.A mechanism for the formation of acrylamide at last was proposed.

Acrylamide formation mechanism in heated foods

L-asparaginase is a vital enzyme of medical importance, and renowned as a chemotherapeutic agent. The relevance of this enzyme is not only limited as an anti-cancer agent, it also possesses a wide range of medical application. The application includes the antimicrobial property, treatment of infectious diseases, autoimmune diseases, canine and feline cancer. Apart from the health care industry, its significance is also established in the food sector as a food processing agent to reduce the acrylamide concentration. L-asparaginase is known to be produced from various bacterial, fungal and plant sources. However, there is a huge market demand due to its wide range of application. Therefore, the industry is still in the search of better-producing source in terms of high yield and low immunogenicity. It can be produced by both submerged and solid state fermentation, and each fermentation process has its own merits and demerits. This review paper focuses on its improved production strategy by adopting statistical experimental optimization techniques, development of recombinant strains, through mutagenesis and nanoparticle immobilization, adopting advanced and cost-effective purification techniques. Available research literature proves the competence and therapeutic potential of this enzyme. Therefore, research orientation toward the exploration of this clinical significant enzyme has to be accelerated. The objectives of this review are to discuss the high yielding sources, current production strategies, improvement of production, effective downstream processing and therapeutic application of L-asparaginase.

Biotechnological production and practical application of L-asparaginase enzyme.

Improvement of paper wastes conversion to bioethanol using novel cellulose degrading fungal isolate

In a natural ecosystem, various organisms digest and hydrolyze lignocellulose biomass efficiently. Termites are one of them. They digest lignocellulose biomass with the help of symbiotic microorganisms in their gut. Therefore, termites gut may harbor potential sources of microorganisms capable to degrade lignocellulose biomass. In this study, termite gut microbiomes of Cryptotermes brevis species were isolated and identified for their capability to degrade lignin and polysaccharides. Alkali lignin, carboxymethylcellulose, and xylan were used as the only carbon sources in the medium to isolate lignin-, cellulose-, and hemicellulose-degrading bacteria. By this method, two bacteria strains, Bacillus sp. BMP01 and Ochrobactrum oryzae BMP03 strain were isolated and identified. Bacillus sp. BMP01 strain has capabilities to hydrolyze carboxymethylcellulose and xylan to glucose and xylose, respectively. This strain showed high xylanase activity (about 0.21 U/ml) and carboxymethyl cellulase activity (about 0.25 U/ml). The ability to hydrolyze both carboxymethylcellulose and xylan makes it superior to other known cellulolytic bacteria. Ochrobactrum oryzae BMP03 strain showed laccase activity, which indicates its ability to depolymerize lignin. Lignocellulose-degrading bacteria play a vital role in the biological conversion of lignocellulose biomass to biofuel. Overall, this study shows that termite’s gut microbiomes are potential sources of lignocellulose-degrading bacteria that can be cultured and used in the biological conversion of lignocellulose biomass to biofuel.

Isolation and Characterization of Novel Lignolytic, Cellulolytic, and Hemicellulolytic Bacteria from Wood-Feeding Termite Cryptotermes brevis

Screening of cellulose degradation bacteria from Min pigs and optimization of its cellulase production

Optimization and molecular identification of novel cellulose degrading bacteria isolated from Egyptian environment

Bacillus pumilus and Bacillus alvei, among alkaline protease producing strains, were used to examine the changes in alkaline protease gene expression following UV irradiation. Induction of mutation in Bacillus mutant strains was carried out by 0, 5, 10, 15 and 20 min. exposure times of UV irradiation and different distances between the treated bacterial cultures and UV source. Results revealed that alkaline protease activity assayed under submerged culture conditions was more accurate than the relative growth production (C/G) method, because there was no proportional correlation between zone diameter and the ability to produce the enzyme in submerged cultures. No enzyme activity was scored with B. pumilus mutants, while the activity was pronounce, in case of B. alvei mutants. Mutants No.15, 55 and 34 were the most efficient in enzyme production under submerged conditions being 68.8, 81.1 and 99 U/ml, respectively. Their alkaline protease activities were 2.6, 3.02 and 3.7 folds than those of the original strains. The optimal enzyme production was achieved after 48 hr at air: medium ratio of 39: 1. Results also proved that the inoculum size in all tested mutant ranges had no significant effect on the enzyme production .The supplementation with glucose to growth medium gave the highest level of enzyme productivity, while lactose showed the lowest. The addition of arabinose and xylose completely inhibited the enzyme production by both tested strains, while incorporation into the culture medium of sucrose and maltose failed to produce the enzyme in B. alvei, but in mutant No.8, they enhanced high levels of productivity.

Induction of overproducing alkaline protease Bacillus mutants through UV irradiation

Improvement of cellulose degradation by cloning of endo-β-1, 3-1, 4 glucanase (bgls) gene from Bacillus subtilis BTN7A strain.

L-asparaginase has been used as a mainstay of all treatment of acute lymphoblastic leukemia. This work amid to improve L-asparaginase production by constructing recombinant overproducing L-asparaginase strains through protoplast fusion technique between two highly L-asparaginase-producer local isolates, i.e., Bacillus subtilis and B. cereus. B. subtilis was sensitive to rifampcin (Rifs) and could utilize L-asparagine as a sole source of nitrogen while Bacillus cereus was resistant to (Rifr), does not grow on minimal medium and can not utilize L-asparagine. Protoplast was induced by treating bacterial cells with 1 mg/ml -1 lysozyme for three hours in SMM buffer. Protoplast regeneration was successfully obtained on sodium-succinate medium where protoplast regeneration rates were 39.8 and 25.6% for Bacillus subtilis and B. cereus, respectively. Protoplast fusion was performed between the two parental protoplasts in the presence of 40% PEG 6000. Fusants were obtained at high frequency, 17.7 x 10 -2 on minimal M9 medium supplemented with rifampcin. Among forty five fusants, 18 showed significant higher L-asparaginase activity, they produced approximately 2.5fold more L-asparaginase. Optimization of physiological and fermentation factors for L-asparaginase overproducers hybrid strains were described. The obtained results indicated that protoplast fusion technique has a great potential for strain improvement particularly those used in industrial application.

L-asparaginase Hyperproducing Recombinant Bacillus Strains Obtained by Interspecific Protoplast Fusion.

The most abundant organic carbon source on Earth is cellulosic materials. Its main resources are crop straws which are not commonly used and produce environmental pollution. These resources can be a site of biological hydrolysis to primary sugars by cellulase enzymes, in which avicelase is the most efficient enzyme in the cellulase family. This work aimed to clone the avicelase gene, transfer it to E. coli, optimize its expression, saccharify rice straw to its primary sugars, and ferment it to bioethanol. The avicelase gene was cloned from the Bacillus subtilis strain and cloned into two E. coli (i.e., DH5α and Bl21) strains. The optimized avicelase activity was described by testing the effect of different media and growth conditions including different carbon and nitrogen sources, as well as pHs and shaking or static conditions. Avicelase enzyme was extracted and used to saccharify rice straw. The obtained glucose was subjected to fermentation by Saccharomyces cerevisiae F.307 under an aerobic condition growth for the production of bioethanol. The ethanol yield was 5.26% (v/v), and the fermentation efficiency was 86%. This study showed the ability to clone one of the cellulolytic genes (i.e., avicelase) for the valorization of rice straw for producing renewable energy and bioethanol from cellulolytic wastes such as rice straw.

https://www.mdpi.com/2571-8797/5/2/23/pdf?version=1681204532

Bio Ethanol Production from Rice Straw Saccharification via Avicelase Gene in E. coli Recombinant Strain

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