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Freshwater and marine diatoms produce the majority of the oxygen in aquatic systems. Estimates range from 12,000 to 30,000 species, and spatial distribution varies globally. There is significant variation in diatom diversity based on geographical and environmental conditions as well as the physicochemical characteristics of the habitat. Therefore, understanding the underlying factors that contribute to changes in diatom community structures requires a comprehensive understanding of taxons. A study of diatom assemblages from the Cambay Basin, Western Arabian Sea, was conducted, particularly on oil fields. A total of 37 samples were collected; nine were from oil fields. We evaluated micro-oil spills using Fourier transform infrared (FTIR) analysis and microscopic techniques. Correlations were established through the ordination analysis of pernicious physical and chemical water variables (BOD, COD, TDS, pH, temperature, and DO), including principal component analysis (PCA). The oil field sites showed more total dissolved solids (TDS) and chemical oxygen demand (COD) than the respective marine control sites. The study does not display a cause-and-effect relationship, but we observed a positive correlation between increasing silica concentrations and diatom growth in oil fields. In contrast, high aluminium concentrations in oil fields negatively impacted the growth of diatom assemblage and abundance. When surveyed in nine oil fields, we found that Gomphonella pseudosphaerophorum and Nitzschia palea are well adapted to oil concentrations up to 40 ppm., (© 2023. The Author(s), under exclusive licence to Springer Nature Switzerland AG.)

The biotechnological application of bacterial xylanases requires a high thermostability, a catalytically active state for a broad pH range. The Bacillus amyloliquefaciens (MTCC 1270) xyn A gene was amplified and cloned into the pCold vector and was expressed in Escherichia coli to evaluate the expressed proteins' thermostability . The pCold, compared to other similar vectors, has unique properties-including pH and temperature tolerance due to the presence of the cspA promoter. The recombinant xyn A-pCold (rxynApC) showed the expression of xyn A gene with a molecular weight of ~ 27 kDa, confirmed on SDS-PAGE. The rxynApC exhibits optimal activity at 70 °C and pH 8.0. The residual activity of the recombinant enzyme was 90% at pH 8.0. The thermal decomposition temperature ( T d ) value for the rxynApC enzyme was 93.33 °C obtained from the thermogravimetric analysis, indicating the potent stability of the cloned enzyme. The specific activity of native xylanase and rxynApC under optimal conditions was 32.35 and 105.5 U/mg, respectively. The structural model of the xyn A gene was predicted using the in silico tool along with the active site (containing four important Tyr-166, Gly-7, Try-69 and Arg-112 amino acids). The predicted biophysical parameters of the in silico model were similar to the experimental results. The unique feature of the csp A promoter is that it gave a high expression of rxynApC enzyme having alkali and thermostable properties with high yield in surrogate host E. coli. Thus, the recombinant xyn A gene can potentially be applied to different industrial needs by looking at its thermostability and enhanced enzyme activity., Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-022-03315-y., Competing Interests: Conflict of interestThe authors declare that they have no conflict of interest in the publication., (© King Abdulaziz City for Science and Technology 2022, Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.)

Industrial processing of enzymes requires higher heating that affects the thermal stability of the enzyme and increases the production cost. In this study, xylanase-phytase (XP) fusion protein was generated via co-expression in a single vector with a cold-shock promoter, leading to improved activity at optimal pH, temperature and the thermal behaviour of the protein. Xylanase-phytase (XP) fusion and phytase proteins were characterized by differential scanning calorimetry (DSC) and thermogravimetric analysis (TGA). The XP fusion was thermally stable up to 124 °C, higher than phytase which was steady up to 113.5 °C. XP fusion exhibits higher stability at its thermal transition midpoint ( T m ) 108 °C, higher than the T m value of phytase which is 90 °C. Industrially efficient and environment-friendly proteins with low production cost and higher stability can be generated by 'fusion protein' technology., Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-021-02936-z., Competing Interests: Conflict of interestThe authors declare that they have no conflict of interest., (© King Abdulaziz City for Science and Technology 2021.)

Agriculture P management practices elevate the level of inorganic phosphates in soil that results in phosphorous (P) seepage into water-bodies. This is one of the key factors that have accelerated the menace of eutrophication. Phytic acid (phytate)-P-rich plant metabolite is infamous for its anti-nutrient activity and regularly oozing in to environment though discharge of mono-gastric animals. That has amplified the magnitudes of eutrophication. In this work, for catalysis of phytate-P, the metal-organic framework fabricated towards metal oxides (Fe 3 O 4 ) and phytase in highly ordered microcosms of silica was employed. The synthesized framework was characterized through transmission electron microscopy (TEM) and nitrogen isotherm analysis. Average pore diameter of synthesized bisect oval shaped structures was measured around ≈200 nm. Herein, phytase and Fe 3 O 4 nanoparticles were loaded to the cavities of microcosms through glutaraldehyde-mediated crosslinking. Whereas Fe 3 O 4 nanoparticles act as nano-absorbents that adsorb P liberated from phytase-mediated catalysis of phytate. Kinetic analysis of free and loaded phytase has shown relatively small reduction in catalytic efficiency. These loaded microcosms have removed 60-80% of phytate-phosphate. The optimized process has reduced the growth of photoautotrophs by 50%. Additionally the magnet-assisted separation of loaded microcosms eased the reapplication of loaded microcosms tested for six independent instances. The primary studies conducted to evaluate the geno-toxicity of loaded microcosms have not shown any harmful effect on the process like cell division and seed germination. The efficacy of this method has evaluated towards on-field testing in Changa (Gujarat, India) lake.