AYODEJI AMOBONYE

Dr. AYODEJI AMOBONYE

Department of Biotechnology and Food Science, Durban University of Technology, Durban, South Africa
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Research Focus & Metrics

Academic Career Length

13Years (2014-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 March 2021 in Science of The Total Environment
Verified
Journal Article
Closed access
AAAYODEJI AMOBONYE
AYODEJI AMOBONYE
PBPrashant Bhagwat
Prashant Bhagwat
SSSuren Singh
Suren Singh
Santhosh PillaiSanthosh Pillai
Santhosh Pillai

10 August 2020 in Critical Reviews in Biotechnology
Verified
Journal Article
Closed access
AAAYODEJI AMOBONYE
AYODEJI AMOBONYE
PBPrashant Bhagwat
Prashant Bhagwat
Ashok PandeyAshok Pandey
Ashok Pandey
SSSuren Singh
Suren Singh
Santhosh PillaiSanthosh Pillai
Santhosh Pillai
Beauveria bassiana though widely perceived as an entomopathogenic fungus has also been found in nature to be endophytic. As entomopathogens, the life cycle of different B. bassiana strains are organized and adapted as pathogens to their invertebrate hosts while as endophytes they maintain a symbiotic relationship with their plant hosts. To fulfill these aforementioned ecological roles, this fungus secretes an array of enzymes as well as secondary metabolites, which all have significant biological roles. Basically, chitinases, lipases and proteases are considered to be the most important of all the enzymes produced by B. bassiana. However, studies have also shown their ability to produce other vital enzymes which include amylase, asparaginase, cellulase, galactosidase etc. Previous reports on this filamentous fungus have laid more emphasis on its entomopathogenicity, its endophytism and its highly acclaimed application in the biological control of pests. This review, however, is the first to fully assess the enzyme-secreting potential of this entomopathogenic fungus and its use as a novel source of several industrial biocatalysts and other important biochemicals. This article highlights the inherent properties of the fungus to degrade various biopolymers as well as its relative safety for human use. Some of the important factors have raised the possibilities of exploitation for industrial production and as safe hosts for gene expression.

9 May 2024 in Biochimie
Verified
Journal Article
Open access
BMBuka Magwaza
Buka Magwaza
AAAYODEJI AMOBONYE
AYODEJI AMOBONYE
Santhosh PillaiSanthosh Pillai
Santhosh Pillai
The global β-glucosidase market is currently estimated at ∼400 million USD, and it is expected to double in the next six years; a trend that is mainly ascribed to the demand for the enzyme for biofuel processing. Microbial β-glucosidase, particularly, has thus garnered significant attention due to its ease of production, catalytic efficiency, and versatility, which have all facilitated its biotechnological potential across different industries. Hence, there are continued efforts to screen, produce, purify, characterize and evaluate the industrial applicability of β-glucosidase from actinomycetes, bacteria, fungi, and yeasts. With this rising demand for β-glucosidase, various cost-effective and efficient approaches are being explored to discover, redesign, and enhance their production and functional properties. Thus, this present review provides an up-to-date overview of advancements in the utilization of microbial β-glucosidases as "Emerging Green Tools" in 21st-century industries. In this regard, focus was placed on the use of recombinant technology, protein engineering, and immobilization techniques targeted at improving the industrial applicability of the enzyme. Furthermore, insights were given into the recent progress made in conventional β-glucosidase production, their industrial applications, as well as the current commercial status-with a focus on the patents.

1 November 2014 in Saudi Journal of Biological Sciences
Verified
Journal Article
Open access
MOMary Tolulope Olaleye
Mary Tolulope Olaleye
AAAYODEJI AMOBONYE
AYODEJI AMOBONYE
KKKayode Komolafe
Kayode Komolafe
AAAfolabi Clement Akinmoladun
Afolabi Clement Akinmoladun
In the present study, we investigated the hepatoprotective potential of Parinari curatellifolia Planch (Chrysobalanaceae) in experimental rats in order to ascertain the validity of folkloric claims of its effectiveness in the treatment of hepatic-related disorders. Flavonoid extract of P. curatellifolia seed, PCF (10-, 20- or 30 mg/kg body weight) or silymarin (25 mg/kg), dissolved in corn oil, was administered by gavage to experimental animals once daily for 14 consecutive days before liver damage was chemically induced through the administration of acetaminophen (2 g/kg p.o.) on the 14th day. Hepatoprotection was assessed by analyzing liver homogenate and serum for markers of hepatotoxicity - alanine aminotransferase (ALT), aspartate aminotransferase (AST), γ-glutamyl transferase (GGT) and lactate dehydrogenase (LDH) activities as well as prothrombin time (PT). Evaluation of biochemical indices of oxidative stress - level of lipid peroxides (LPO), activities of superoxide dismutase (SOD) and catalase, along with histological assessment of hepatic tissue sections were also carried out. Results revealed that all doses of PCF significantly (P < 0.001) and dose dependently prevented acetaminophen-induced increase in serum activities of hepatic enzymes (ALT, AST, GGT, LDH) and PT. Furthermore, PCF (10- and 20 mg/kg) significantly (P < 0.001) reduced lipid peroxidation in liver tissue and restored the activities of the antioxidant enzymes SOD and catalase toward normal levels. Histopathology of the liver tissue showed that PCF mitigated the toxicant-induced hepatocellular necrosis, reduced inflammatory cell infiltration and enhanced hepatocyte regeneration. The results indicated that P. curatellifolia flavonoids demonstrated remarkable hepatoprotective activity in acute liver injury caused by acetaminophen.

22 July 2019 in Critical Reviews in Biotechnology
Verified
Journal Article
Closed access
AAAYODEJI AMOBONYE
AYODEJI AMOBONYE
SSSuren Singh
Suren Singh
Santhosh PillaiSanthosh Pillai
Santhosh Pillai
This article focuses on significant advances in the production and applications of microbial glutaminases and provides insight into the structures of different glutaminases. Glutaminases catalyze the deamidation of glutamine to glutamic acid, and this unique ability forms the basis of their applications in various industries such as pharmaceutical and food organizations. Microbial glutaminases from bacteria, actinomycetes, yeast, and fungi are of greater significance than animal glutaminases because of their stability, affordability, and ease of production. Owing to these notable benefits, they are considered to possess considerable potential in anticancer and antiviral therapy, flavor enhancers in oriental foods, biosensors and in the production of a nutraceutical theanine. This review also aims to fully explore the potential of microbial glutaminases and to set the pace for future prospects.