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The CREA gene has been implicated in glucose repression in several fungi. The product of this gene, CreA, binds to the promoter region of several enzymes and down-regulates gene expression. An ortholog of CREA was isolated and characterized from the maize pathogenic fungus, Cochliobolus carbonum . The deduced amino acid sequence of the C. carbonum CREA gene is very similar to the CreA proteins of Aspergillus niger , Gibberella fujikuroi , Sclerotinia sclerotiorum and Trichoderma reesei , as well as the Mig1 protein of Saccharomyces cerevisiae . And like the other fungal proteins, C. carbonum CreA has two zinc finger regions and a nuclear localization signal. Putative CreA binding sequences were also identified in the 5′ region of three C. carbonum cell wall degrading enzyme genes suggesting that the protein may play a role in the regulatory process that controls these enzymes expression. [ABSTRACT FROM AUTHOR]

To meet the growing demand for L-lysine, an essential amino acid with various applications, it is crucial to produce it on a large scale locally instead of relying solely on imports. This study aimed to evaluate the potential of using Corynebacterium glutamicum ATCC 13032 for L-lysine production from agricultural by-products such as palm kernel cake, soybean cake, groundnut cake, and rice bran. Solid-state fermentation was conducted at room temperature for 72 h, with the addition of elephant grass extract as a supplement. The results revealed that these agricultural by-products contain residual amounts of L-lysine. By employing solid-state fermentation with C. glutamicum (106 CFU/ml) in 100 g of various agricultural by-products, L-lysine production was achieved. Interestingly, the addition of elephant grass extract (1 g of elephant grass: 10 ml of water) further enhanced L-lysine production. Among the tested substrates, 100 g of groundnut cake moistened with 500 ml of elephant grass extract yielded the highest L-lysine concentration of 3.27 ± 0.02 (mg/gds). Furthermore, fermentation led to a substantial rise (p < 0.05) in soluble protein, with solid-state fermented soybean cake moistened with 500 ml of elephant grass extract exhibiting the highest amount of 7.941 ± 0.05 mg/gds. The activities of xylanase, amylase and protease were also significantly enhanced. This study demonstrates a viable biotechnological approach for locally producing L-lysine from agricultural by-products using solid-state fermentation with C. glutamicum. The findings hold potential for both health and industrial applications, providing a sustainable and economically feasible method for L-lysine production. [ABSTRACT FROM AUTHOR]

Solid-state fermentation (SSF) is a promising technology for producing value-added products from cassava (Manihot esculenta Crantz). In this process, microorganisms are grown on cassava biomass without the presence of free-flowing liquid. Compared to other processing methods, SSF has several advantages, such as lower costs, reduced water usage, and higher product yields. By enhancing the content of bioactive compounds like antioxidants and phenolic compounds, SSF can also improve the nutritional value of cassava-based products. Various products, including enzymes, organic acids, and biofuels, have been produced using SSF of cassava. Additionally, SSF can help minimize waste generated during cassava processing by utilizing cassava waste as a substrate, which can reduce environmental pollution. The process has also been explored for the production of feed and food products such as tempeh and cassava flour. However, optimizing the process conditions, selecting suitable microbial strains, and developing cost-effective production processes are essential for the successful commercialization of SSF of cassava. [ABSTRACT FROM AUTHOR]

The biochemical parameters of solid-state fermented peeled and unpeeled cassava roots (Manihot esculenta Crantz) and their application in broiler feed formulations were investigated. Fermentation occurred at room temperature for 72 h (pH 3—9). The samples utilized for five (5) broiler starter feeds were labeled: control, unfermented unpeeled cassava (UUC), unfermented peeled cassava (UPC), fermented unpeeled cassava (FUC), and fermented peeled cassava (FPC). Formulations were made by substituting fermented/non-fermented cassava roots at pH 7 for maize (w/w%). Fermentation-induced changes included increased soluble and total protein concentrations (69.3 and 334.5 mg/g) and (9.6 and 10.8%), respectively, in cultures prepared with peeled and unpeeled cassava at pH 7 compared to the control (p < 0.05), and a reduction (p < 0.01) in cyanide concentration from 44.4 to 78.7 mg/kg in the control to 8.5 and 13.7 mg/kg in fermented cassava at pH 7. Birds fed FUC and FPC meal (0.6 and 0.5 kg) gained significantly more weight (p < 0.05) than those fed the control (0.3 kg). The biochemical parameters aspartate aminotransferase (AST), alanine aminotransferase (ALT), creatinine, and urea levels in broiler serum did not differ significantly (p > 0.05) for birds fed with fermented peeled and unpeeled cassava. Conversely, serum albumin and calcium levels were significantly lower (p < 0.05) for birds fed with the control feed compared to birds fed with fermented feeds. The results imply that fermented peeled and unpeeled cassava roots could be a safe and nutritionally beneficial replacement for maize in broiler diet. [ABSTRACT FROM AUTHOR]

Electronic publishing has been heralded as a worldwide solution to information dissemination. This article considers the current problems experienced by traditional journals published in the developing world, with particular reference to publishing in sub-Saharan Africa. The opportunities offered by electronic online publishing are discussed to determine how they can resolve the current problems in dissemination and improve quality Two case studies of different initiatives are presented: an online-only journal, the African Journal of Biotechnology (AJB), and an online journal abstracting service, African Journals OnLine (AJOL). The article concludes that although online publishing is not a solution for all the problems experienced by journals in developing countries, it offers great potential for increasing the visibility and quality of indigenous knowledge within the global research community. [ABSTRACT FROM AUTHOR]

• Fluorescence,3D,Syn,UV–vis,FT-IR,Mol.Docking affirmed BSA-LVG interaction. • BSA intrinsic fluorescence was quenched by LVG via static mechanism. • LVG binding altered BSA native conformation. • Site probing, Mol.Docking revealed LVG at interface of BSA subdomains IIA & IIIA. • ASC, SAL suppressed BSA binding affinity for levonorgestrel. Serum proteins generally help to transport and distribute drug molecules within the body. In this study, the binding characteristics of bovine serum albumin (BSA) with levonorgestrel (LVG), an emergency contraceptive pill, and the influences of ascorbic acid (ASC) and salicylic acid (SAL) on the binding behaviour and protein structure were elucidated using multi-spectroscopic techniques and molecular docking. The results showed that levonorgestrel decreased BSA intrinsic fluorescence via static quenching mechanism. Binding constant (K a) values for BSA-LVG complexes were 103 to 104 M-1, indicating their high stabilities. Site probing/docking analysis indicated LVG bound between BSA subdomains IIA and IIIA. UV–visible absorption, Fourier Transform-Infrared and 3D fluorescence spectroscopies affirmed LVG-induced changes in BSA structure, especially in α-helix and β-sheet contents. ASC and SAL influenced BSA conformation for LVG binding and reduced the K a values by 3.37 and 5.43-folds, respectively. LVG altered the microenvironments of tyrosine residues, interacted with Arg-217, Lys-221, Val-292, Glu-443 etc. within the binding domains. The process was spontaneous (ΔG<0), entropy driven (TΔS>ΔH) and involved van der Waals forces and hydrogen bonding. The findings of the study offered details on the binding interaction between BSA and LVG, and also indicated that prior intake of ASC or SAL could suppress the binding affinity of BSA for levonorgestrel. [Display omitted] [ABSTRACT FROM AUTHOR]

[Display omitted] • Kinetics, fluorescence, UV–Vis, FT-IR, Mol. Docking affirmed α-amylase-CA interaction. • CA inhibited α-amylase activity by a mixed inhibition, K ic < K iu ; with moderate IC 50. • AMY intrinsic fluorescence was quenched by CA via static mechanism. • CA binding altered AMY native conformation. • CA suppressed Advanced Glycation End-products (AGEs) formation. The quest to suppress complications associated with diabetes mellitus is ever increasing, while food additives and preservatives are currently being considered to play additional roles besides their uses in food enhancement and preservation. In the present study, the protective prowess of a common food preservative (citric acid, CA) against advanced glycation end-products (AGEs) formation and its binding interaction mechanism with α-amylase (AMY), an enzyme linked with hyperglycemia management, were examined. Enzyme inhibition kinetics, intrinsic fluorescence, synchronous and 3D fluorescence spectroscopies, ultraviolet–visible (UV–Vis) absorption spectroscopy, Fourier transform-infrared (FT-IR) spectroscopy, thermodynamics, and molecular docking analyses were employed. Results obtained showed that citric acid decreased α-amylase activity via mixed inhibition (IC 50 = 5.01 ± 0.87 mM, K ic = 2.42 mM, K iu = 160.34 mM) and suppressed AGEs formation (IC 50 = 0.795 ± 0.001 mM). The intrinsic fluorescence of free α-amylase was quenched via static mechanism with high bimolecular quenching constant (K q) and binding constant (K a) values. Analysis of thermodynamic properties revealed that AMY-CA complex was spontaneously formed (ΔG < 0), entropy driven (TΔS > ΔH), with involvement of electrostatic forces. UV–Vis, FT-IR and 3D fluorescence spectroscopies affirmed alterations in α-amylase native conformation due to CA binding interaction. CA interacted with His-101, Asp-197, His-299, and Glu-233 within AMY active site. Our findings indicated that CA could impair formation of AGEs and interact with α-amylase to slow down starch hydrolysis; vital properties in management of type 2 diabetes complications. [ABSTRACT FROM AUTHOR]

East Coast fever, caused by the tick-borne intracellular apicomplexan parasite Theileria parva, is a highly fatal lymphoproliferative disease of cattle. The pathogenic schizont-induced lymphocyte transformation is a unique cancer-like condition that is reversible with parasite removal. Schizont-infected cell-directed CD8+ cytotoxic T lymphocytes (CTL) constitute the dominant protective bovine immune response after a single exposure to infection. However, the schizont antigens targeted by T. parva-specific CTL are undefined. Here we show the identification of five candidate vaccine antigens that are the targets of MHC class I-restricted CD8+ CTL from immune cattle. CD8+ T cell responses to these antigens were boosted in T. parva-immune cattle resolving a challenge infection and, when used to immunize naïve cattle, induced CTL responses that significantly correlated with survival from a lethal parasite challenge. These data provide a basis for developing a CTL-targeted anti-East Coast fever subunit vaccine. In addition, orthologs of these antigens may be vaccine targets for other apicomplexan parasites. [ABSTRACT FROM AUTHOR]

Obesity is a global health problem characterized by excessive fat deposition in adipose tissues and can be managed by targeting pancreatic lipase (PL) activity. In the present study, we investigated the in vitro antioxidant and anti-obesity potentials of methanolic leaf extract of Justicia carnea (MEJC) using lipase inhibition kinetics model. In silico evaluations of MEJC bioactive compounds as potential drug-like agents and inhibitors of PL were also investigated using SwissADME prediction tool, semi-empirical quantum mechanics(SQM), molecular electrostatic potential(MEP) and molecular docking analysis. Gas chromatography-mass spectrometry(GC–MS) revealed presence of campesterol, stigmasterol, beta-amyrin etc. MEJC scavenged reactive species and inhibited PL activity via a mixed inhibition pattern (K i = 107.69 μg/mL; K ii = 398.00 μg/mL) with IC 50 > orlistat's IC 50. Molecular docking of GC–MS identified compounds with porcine PL showed compounds 8,10,12 and 14 having high PL-binding affinity and similar binding pose with orlistat. Hydrophobic interactions and van der Waals forces were predominantly involved in the ligands' interactions with some key catalytic site amino acid residues (Ser-153,His-264). Compounds 10 , 12,13 and 14 indicated high drug-likeness, bioavailability, electronegativity, E LUMO -E HOMO energy gaps and MEP. Our findings show that MEJC is a rich natural source of antioxidant and anti-obesity agents which could be optimized for development of new anti-obesity drugs. [Display omitted] • Kinetics,SQM, MEP, Molecular docking gave evidence of lipase interaction with MEJC. • MEJC exhibited antioxidant properties. • MEJC inhibited pancreatic lipase by mixed inhibition pattern. • Compounds 10 , 12,13 and 14 showed high drug-likeness and chemical reactivity. • MEJC could be a potential source of novel lipase inhibitors. [ABSTRACT FROM AUTHOR]

The present study investigated the antioxidant and in vitro antidiabetic capacities of Justicia carnea aqueous leaf extract (JCAE) using α-amylase inhibition model. α-Amylase binding-interaction with JCAE was also investigated using fluorescence spectroscopy and molecular docking. Phytochemical screening and Gas Chromatography-Mass Spectrometry (GC–MS) analysis indicated presence of bioactive compounds. Phenolic (132 mg GAE/g) and flavonoid contents (31.08 mg CE/g) were high. JCAE exhibited high antioxidant capacity and effectively inhibited α-amylase activity (IC 50 , 671.43 ± 1.88 μg/mL), though lesser than acarbose effect (IC 50 , 108.91 ± 0.61 μg/mL). α-Amylase intrinsic fluorescence was quenched in the presence of JCAE. Ultraviolet-visible and FT-IR spectroscopies affirmed mild changes in α-amylase conformation. Synchronous fluorescence analysis indicated alterations in the microenvironments of tryptophan residues near α-amylase active site. Molecular docking affirmed non-polar interactions of compounds 6 and 7 in JCAE with Asp-197 and Trp-58 residues of α-amylase, respectively. Overall, JCAE indicated potential to prevent postprandial hyperglycemia by slowing down carbohydrate hydrolysis. Unlabelled Image • UV–vis, FT-IR and fluorescence provide evidence of α-amylase interaction with JCAE. • JCAE inhibited α-amylase activity and quenched α-amylase intrinsic fluorescence. • Microenvironments of tryptophan residues near α-amylase active site were altered. • Compounds 6 and 7 in JCAE showed highest binding affinities to α-amylase. • JCAE could be a potential source of novel α-amylase inhibitors. [ABSTRACT FROM AUTHOR]