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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]

• 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]