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Polyurethane (PU) is a plastic polymer which, due to its various desirable characteristics, has been applied extensively in domestic, industrial and medical fields for the past 50 years. Subsequently, an increasing amount of PU waste is generated annually. PU, like many other plastics, is highly resistant to degradation and is a substantial threat to our environment. Currently PU wastes are handled through conventional disposal techniques such as landfill, incineration and recycling. Due to the many drawbacks of these techniques, a 'greener' alternative is necessary, and biodegradation appears to be the most promising option. Biodegradation has the potential to completely mineralise plastic waste or recover the input materials and better enable recycling. There are hurdles to overcome however, primarily the efficiency of the process and the presence of waste plastics with inherently different chemical structures. This review will focus on polyurethanes and their biodegradation, outlining the difficulty of degrading different versions of the same material and strategies for achieving more efficient biodegradation., (© 2023. The Author(s).)

Azospirillum lipoferum MTCC 2306, a free-living nitrogen fixing bacteria, has a doubling time of 1.7 h in MPSS media. At the end of 28 h at a pH of 7 and temperature of 30 °C it produces 1.8 ± 0.013 g/L biomass and 2.1 ± 0.018 g/L of cyclic beta glucan (CβG) in MPSS medium with a yield coefficient (Y P/S ) of 2.1. This novel polysaccharide is a water-soluble cyclic biopolymer and is generally produced by Rhizobiaceae and predominantly made up of glucose. The CβG has a degree of polymerisation varying between 10 and 13 and has both α- and β-glycosidic linkages. It is not substituted with any functional groups such as acetates or succinates. Its ability to bind to aniline blue suggests that it can be a potential candidate for being used as carrier in medical imaging as well as in reducing toxicity of textile effluents. It is able to encapsulate rifampicin, a hydrophobic drug and increase its aqueous solubility by 71%. So, CβG appears to have promising applications in the field of drug, food, cosmetic and nutraceutical industries.

Antimicrobial peptides (AMPs) have been established over millennia as powerful components of the innate immune system of many organisms. Due to their broad spectrum of activity and the development of host resistance against them being unlikely, AMPs are strong candidates for controlling drug-resistant pathogenic microbial pathogens. AMPs cause cell death through several independent or cooperative mechanisms involving membrane lysis, non-lytic activity, and/or intracellular mechanisms. Biochemical determinants such as peptide length, primary sequence, charge, secondary structure, hydrophobicity, amphipathicity and host cell membrane composition together influence the biological activities of peptides. A number of biophysical techniques have been used in recent years to study the mechanisms of action of AMPs. This work appraises the molecular parameters that determine the biocidal activity of AMPs and overviews their mechanisms of actions and the diverse biochemical, biophysical and microscopy techniques utilised to elucidate these.

Drug-resistant microorganisms ('superbugs') present a serious challenge to the success of antimicrobial treatments. Subsequently, there is a crucial need for novel bio-control agents. Many antimicrobial peptides (AMPs) show a broad-spectrum activity against bacteria, fungi or viruses and are strong candidates to complement or substitute current antimicrobial agents. Some AMPs are also effective against protozoa or cancer cells. The tryptophan (Trp)-rich peptides (TRPs) are a subset of AMPs that display potent antimicrobial activity, credited to the unique biochemical properties of tryptophan that allow it to insert into biological membranes. Further, many Trp-rich AMPs cross bacterial membranes without compromising their integrity and act intracellularly, suggesting interactions with nucleic acids and enzymes. In this work, we overview some archetypal TRPs derived from natural sources, i.e., indolicidin, tritrpticin and lactoferricin, summarising their biochemical properties, structures, antimicrobial activities, mechanistic studies and potential applications.

Peptides modelled on the tryptophan rich domain of puroindolines and the related grain softness protein-1 have a broad range of antibacterial and antifungal activities. With the aims of further investigating the activities of these antimicrobial peptides we studied their activity against wheat rust diseases and environmental stability. PINA-based peptides were found to have high pH and thermal stability in addition to being stable over long periods at room temperature. These properties could make them excellent candidates as preservatives in food. PuroA, Pina-R39G and PuroB peptides adversely affected the morphology of the stripe rust spores (Puccinia striiformis f. sp. tritici), while PuroA and PuroB showed moderate inhibition of their germination. Additionally, GSP-5D reduced the germination of leaf rust spores (P. triticina). PuroA and PuroB sprayed onto stripe rust infected plants effected a moderate reduction in the number of stripe rust uredinia on wheat seedlings, as did PuroB sprayed onto the seedlings and allowed to coat the leaves for 5 day prior to spore infection. The results suggest that the presence of the PIN-based peptides may lower frequency of initial infection foci.

A number of human activities result in environmental contamination with copper compounds that can cause severe detrimental effects on the ecosystem as well as human health. The physico-chemical methods of metal detection have limitations such as inability to distinguish between total versus bio-available metals and differences in metal uptake in different organisms. The heavy metal resistance-encoding genetic systems of certain bacteria provide critical tools for development of biosensors for these purposes. This study reports a copper biosensor utilizing the cop operon of the heavy metal resistant bacterial isolate, Achromobacter sp. AO22, isolated from a contaminated site in Australia. A section located between the divergently transcribed putative response regulator gene copR and multicopper oxidase gene copA that included a palindromic cop box was identified as a copper-responsive promoter using a lacZ reporter construct, pCOPRP, in E. coli. The expression was found to be enhanced by inclusion of copR. Another engineered strain, AO22(pCOPRP), showed stronger induction, and the lacZ expression in both backgrounds was enhanced significantly (250-400 fold) by copper but minimally by other metals. The construct in Achromobacter sp. AO22 thus has a high potential as biosensor for detecting copper bioavailability (hence potential toxicity) in a soil bacterial background, while the construct in E. coli is ideal for laboratory-based testing.

Aquaporins are water channel proteins that control the flow of water across cellular membranes and play vital roles in all aspects of plant-water relations. Our previous identification of 35 wheat PIP and TIP aquaporin genes showed they formed a large family with many conserved features that are thought to be important in structure and function. The present work focussed on determining the positions of these genes in the wheat genome in order to help investigate their functions in water uptake and transport. Genomic locations of wheat PIPs and TIPs were predicted using a number of reported rice-wheat comparative maps and additional in silico approaches. Physical mapping of select genes utilising aneuploid stocks and progenitor DNAs placed these on chromosomes 2B, 2D, 6B and 7B and helped to clarify the individual genes and homoeologues. The compilation of all in silico and physical mapping work confirmed many of the orthologous relationships between wheat and rice and/or barley genes, and synteny in the related areas of genome. These results further reinforce that wheat PIP and TIP proteins are most likely to have similar functions to those closely related in rice, including water permeability and abiotic stress response, and provide important tools for future investigations into the involvement of this complex gene family in traits related to plant-water relations and osmotic stress response.

Aquaporins, members of major intrinsic proteins (MIPs), transport water across cellular membranes and play vital roles in all organisms. Adversities such as drought, salinity, or chilling affect water uptake and transport, and numerous plant MIPs are reported to be differentially regulated under such stresses. However, MIP genes have been not yet been characterized in wheat, the largest cereal crop. We have identified 24 PIP and 11 TIP aquaporin genes from wheat by gene isolation and database searches. They vary extensively in lengths, numbers, and sequences of exons and introns, and sequences and cellular locations of predicted proteins, but the intron positions (if present) are characteristic. The putative PIP proteins show a high degree of conservation of signature sequences or residues for membrane integration, water transport, and regulation. The TIPs are more diverse, some with potential for water transport and others with various selectivity filters including a new combination. Most genes appear to be expressed as expressed sequence tags, while two are likely pseudogenes. Many of the genes are highly identical to rice but some are unique, and many correspond to genes that show differential expression under salinity and/or drought. The results provide extensive information for functional studies and developing markers for stress tolerance.

The ubiquitous cell membrane proteins called aquaporins are now firmly established as channel proteins that control the specific transport of water molecules across cell membranes in all living organisms. The aquaporins are thus likely to be of fundamental significance to all facets of plant growth and development affected by plant-water relations. A majority of plant aquaporins have been found to share essential structural features with the human aquaporin and exhibit water-transporting ability in various functional assays, and some have been shown experimentally to be of critical importance to plant survival. Furthermore, substantial evidence is now available from a number of plant species that shows differential gene expression of aquaporins in response to abiotic stresses such as salinity, drought, or cold and clearly establishes the aquaporins as major players in the response of plants to conditions that affect water availability. This review summarizes the function and regulation of these genes to develop a greater understanding of the response of plants to water insufficiency, and particularly, to identify tolerant genotypes of major crop species including wheat and rice and plants that are important in agroforestry.

The storage protein polymers in the endosperm, stabilised by disulphide bonds, determine a number of processing qualities of wheat dough. The enzyme protein disulphide isomerase (PDI), involved in the formation of disulphide bonds, is strongly suggested to play a role in the formation of wheat storage protein bodies. Reports of the rice mutant esp2 exhibiting aberrant storage protein deposition in conjunction with a lack of PDI expression provided strong indications of a direct role for PDI in storage protein deposition. The potential significance of wheat PDI prompted the present studies into exploring any orthology between wheat PDI genes and rice PDI and esp2 loci. By designing allele-specific (AS)-polymerase chain reaction (PCR) markers, two of the three wheat PDI genes could be genetically mapped to group 4 chromosomes and showed close association with GERMIN genes. Physical mapping led to localisation of wheat PDI genes to chromosomal "bins" on the proximal section of chromosome 4AL and distal sections of 4BS and 4DS. Identification of the putative PDI gene of rice and its comparison to the esp2 locus revealed that they were present at similar positions on the short arm of chromosome 11. Analysis of a large section of the PDI-containing section of rice chromosome 11S revealed a number of putative orthologues from The Institute for Genomic Research Triticum aestivum Gene Index database, of which five had been mapped, each localising to group 4 chromosomes, many in good agreement with our mapping results. The results strongly suggest a close linkage between the esp2 marker and the PDI gene of rice and an orthology between the PDI loci of rice and wheat and predict quantitative-trait loci involved in storage protein deposition at the PDI loci.