A novel pig feed formulation containing Aspergillus niger CSA35 pretreated-cassava peels and its effect on growth and selected biochemical parameters of pigs

This study investigated the effects of Aspergillus niger CSA35 pretreated-cassava (Manihot esculenta Crantz) peel feed (CPFG) on the body weight gain and some selected biochemical parameters of pigs. Cassava peels treated with biomass of A. niger CSA35 for a period of three weeks to initiate enzymatic digestion of peels were dried, ground and used in varying proportions to formulate pig rations in combination with other feed ingredients. Twenty 85–95 days old pigs (5.85 ± 0.70 kg) were randomly divided into four experimental groups. Group 1 received 0% CPFG amidst other feed ingredients (control), while Groups 2, 3 and 4 received 40%, 60% and 100% CPFG respectively. At the end of the feeding trial (21 days), the animals were weighed and blood samples collected for biochemical analysis. Results showed that increasing the amount of the fungus-pretreated cassava peels in pig rations increased the protein, fat and carbohydrate contents of the experimental feeds. Conversely, the percentage fibre content was reduced. The weight gain of pigs fed the control diet was significantly (p<0.05) lower than those fed with 60% CPFG and 100% CPFG but did not differ from those fed 40% CPFG. Serum calcium and albumin levels were observed to be significantly lower (p<0.05) in control group than in treatment groups. The highest serum calcium level was, however, observed in 100% CPFG group. Activities of liver function enzymes and serum creatinine level of pigs fed the formulated diets did not significantly differ from those of control unlike their serum urea levels. It was concluded that pig feeds formulated with cassava peels pretreated with A. niger CSA35 enhanced feed’s nutritive value and metabolisable energy, boosted serum albumin and calcium levels in pigs, increased pigs body weight and are health-friendly since the feeds did not pose threat of liver damage in the pigs investigated.Key words: Cassava peels, Aspergillus niger CSA35, pig feed formulation, weight gain, biochemical parameters

Biochemical characterization of solid-state fermented cassava roots (Manihot esculenta Crantz) and its application in broiler feed formulation

DATA AVAILABILTY : The availability of experimental data would be subject to reasonable request.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) 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.https://link.springer.com/journal/112742023-12-29hj2023Consumer ScienceFood Scienc

Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular docking

regulation of α-amylase activity is now becoming a promising management option for type 2 diabetes. The present study investigated the binding interactions of three structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase to ascertain the affinity of the ligands for α-amylase using spectroscopic and molecular docking methods. The ligands were characterized using 1H and 31P NMR spectroscopy and CHN analysis. Diselenoimidodiphosphinate ligand (DY300), dithioimidodiphosphinate ligand (DY301), and thioselenoimidodiphosphinate ligand (DY302) quenched the intrinsic fluorescence intensity of α-amylase via a static quenching mechanism with bimolecular quenching constant (Kq) values in the order of x1011 M-1s-1, indicating formation of enzyme-ligand complexes. A binding stoichiometry of n≈1 was observed for α-amylase, with high binding constants (Ka). α-Amylase inhibition was as follow: Acarbose > DY301>DY300>DY302. Values of thermodynamic parameters obtained at temperatures investigated (298, 304 and 310 K) revealed spontaneous complex formation (ΔG<0) between the ligands and α-amylase; the main driving forces were hydrophobic interactions (with DY300, DY301, except DY302). UV–visible spectroscopy and F¨orster resonance energy transfer (FRET) affirmed change in enzyme conformation and binding occurrence. Molecular docking revealed ligands interaction with α-amylase via some key catalytic site amino acid residues (Asp197, Glu233 and Asp300). DY301 perhaps showed highest α-amylase inhibition (IC50, 268.11 ± 0.74 μM) due to its moderately high affinity and composition of two sulphide bonds unlike the others. This study might provide theoretical basis for development of novel α-amylase inhibitors from dichalcogenoimidodiphosphinate ligands for management of postprandial hyperglycemia

a-Amylase inhibition, anti-glycation property and characterization of the binding interaction of citric acid with a-amylase using multiple spectroscopic, kinetics and molecular docking approaches

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 a-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 a-amylase activity via mixed inhibition (IC50 = 5.01 ± 0.87 mM, Kic = 2.42 mM, Kiu = 160.34 mM) and suppressed AGEs formation (IC50 = 0.795 ± 0.001 mM). The intrinsic fluorescence of free a-amylase was quenched via static mechanism with high bimolecular quenching constant (Kq) and binding constant (Ka) values. Analysis of thermodynamic properties revealed that AMY-CA complex was spontaneously formed (DG DH), with involvement of electrostatic forces. UV–Vis, FT-IR and 3D fluorescence spectroscopies affirmed alterations in aamylase 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 a-amylase to slow down starch hydrolysis; vital properties in management of type 2 diabetes complications

Isolation, identification and in silico analysis of alpha-amylase gene of Aspergillus niger strain CSA35 obtained from cassava undergoing spoilage

In this investigation, a gene (CDF_Amyl) encoding extracellular α-amylase in Aspergillus niger strain CSA35 associated with cassava spoilage was amplified using specific primers and characterized in silico. The gene had a partial nucleotide sequence of 968 bp and encoded a protein of 222 aa residues with a molecular weight and isoelectric point of 25.13 kDa and 4.17, respectively. Its catalytic site was located in the active site domain. BLASTp analysis showed that the protein primary sequence of the α-amylase gene had 98% and 99% homologies with the α-amylase of A. niger and A. oryzae RIB40, respectively. The gene is more closely related to α-amylase genes from fungi than to bacterial, plant, or animal α-amylase genes. Restriction mapping of the gene showed it can be digested with restriction enzymes like NcoI, PstI, SmaI, and BcLI among others but not with EcoRI and EcoRV. Its protein product had a hydrophobicity score of − 0.43 but no transmembrane helix. The CDF_Amyl protein was subcellularly localized in the secretory pathway, an indication of its release into extracellular space after secretion. Also, the 3D structure of the CDF-Amyl protein was barrel-shaped with domains characteristic of α-amylases. The encoded α-amylase Vmax is 6.90 U/mg protein and Km is 6.70 mg/ml. It was concluded that the unique characteristics of the CDF_Amyl gene and its deduced protein could find applications in biotechnological, food and pharmaceutical industries where cloning and further modification of this gene would be required for product development and improvement

Antigenotoxicity and antioxidant activities of bitter leaf (Vernonia amygdalina del.) accessions from different parts of Nigeria

Bitter leaf (Vernonia amygdalina Del.) plant is a tree species that is highly cultivated in Nigeria for its nutritive and therapeutic values. This study aimed to determine the antioxidant and antigenotoxicity effects (in vitro) of 52 accessions of V. amygdalina collected from six geopolitical zones of Nigeria (North East, North West, North Central, South South, East and West) by evaluating the 2,2-diphenyl-1-picrylhydrazyl (DPPH) and nitric oxide (NO-) scavenging antioxidant activities, flavonoid and phenolic contents as well as ethidium bromide-induced DNA (deoxyribonucleic acid) damage of bitter leaf. The results showed that accessions MN628016 (Oshimili South, Delta State) and MN628010 (Akoko Edo, Edo State), respectively had higher amounts of flavonoid (287.19 mg/g/FW) and phenolic (307.90 mg/g/FW) contents. The accessions MN627984 (Ikpoba Okha, Edo State) and MN627975 (Owerri, Imo State) had the highest nitric oxide (85.73%) and DPPH radical scavenging inhibitory effect (98.92%). The highest percentage fragmented DNA (45.05%), was observed in Allium cepa roots homogenised and mixed with ethidium bromide followed by the A. cepa roots homogenised and mixed with the leaf extract of V. amygdalina accession MN627977 (36.12%). However, V. amygdalina accessions MN628008 (457.62%, Warri North, Delta State) had the highest percentage increase of fragmented DNA followed by MN628024 (395.04%, Oshimili North, Delta State), MN628015 (345.54%; Aniocha North, Delta State) and MN627984 (342.04%; Ikpoba Okha, Edo State) while accession MN628010 (7.32%; Akoko Edo, Edo State) had the lowest. Accession MN628010 which possessed the highest amount of phenolic content had the lowest percentage increase of fragmented DNA and accession MN627984 which possessed the highest nitric oxide radical scavenging inhibitory effect was among the accessions with the highest percentage increase of fragmented DNA. The findings of this study suggest that the observed lowest percentage of fragmented DNA of A. cepa roots growth induced with the solution of ethidium bromide and treated with V. amygdalina accessions MN628010 extracts (antigenotoxic) could be as a result of the high antioxidant activities in the V. amygdalina accessions. In summary, the findings of this study showed that the 52 V. amygdalina accessions obtained from different locations of Nigeria will help to combat ethidium bromide induced genoxicities and any other genotoxicant that may lead to different complications in plant (A. cepa roots), as all the accessions possessed antioxidant and antigenotoxic properties, as such, possessed comparable amount of natural antioxidant activities and antigenotoxicity

Nutritional compositions and antioxidant properties of typical Urhobo Nigerian soups

In this study, the nutritional compositions and antioxidant properties of six typical Urhobo (Nigerian) soups; Amiedi (Elaeis guineensis extract), Palm oil (‘Oghwo-evwri’), Egusi (Citrullus lanatus)–Okro (Abelmoschus esculentus) soup (‘Emuigari-ishavwo’), Pepper (Iribo-erhare), Egusi-vegetable (‘Emuigarifo’), and Egusi-Pepper (‘Ovwovwo’) were investigated. The results show that the typical Urhobo soups were rich in protein and contained extremely low concentrations of reducing sugars. The highest concentrations of high density lipoprotein (HDL)-cholesterol (7.35 ± 0.25 mg/ml), low density lipoprotein (LDL)-cholesterol (1.19 ± 0.67 mg/ml), and triglycerides (6.67 ± 0.29 mg/ml) were observed in ‘Ovwovwo’, ‘Amiedi’ and ‘Emuigari ishavwo’, respectively. The 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging assay results showed that all the soup samples exhibit high antioxidant properties. Also, the highest radical scavenging effect was observed in Amiedi and Emuigari-ishavwo soups. The high amount of phenolic and flavonoid compounds in the soups is a measure of their antioxidant capacities. The soups are not only nutritious but also health protective. Keywords: Typical Urhobo soups, Nutritional compositions, Phenols, Flavonoids, DPPH radical, Antioxidant activityNigerian Journal of Technological Research, 8(2), 201