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European Journal of Applied Sciences – Vol. 9, No. 5
Publication Date: October 25, 2021
DOI:10.14738/aivp.95.11036. Agwu, C. H. (2021). Molecular Screening and Production of α-amylase from Fungal sp. European Journal of Applied Sciences, 9(5).
365-379.
Services for Science and Education – United Kingdom
Molecular Screening and Production of α-amylase from Fungal sp
Agwu Cletus H.
National agency for Food and Drug Administration and Control
Enugu division
ABSTRACT
α-amylase producing Aspergillus sp. was isolated from decaying bread collected
from bakery site located within Enugu metropolis, Enugu state. Standard
microbiology, biochemical and molecular techniques (18s DNA sequencing) were
used for confirmation of the fungal strain as Aspergillus tamari.. p-NPG infused
nutrient broth confirmed Aspergillus tamarrii as prolific producer of α-amylase
with rapid yellow colouration after forty eight hours of incubation. Solid state
fermentation on rice bran matrix (SSF) system was used for the enzyme production.
Cork borer of 2mm diameter was used throughout the production and optimization
studies. Carbon sources including: Starch, wheatbran and sugarcane baggase were
optimized, starch was found suitable for the protein production with highest α- amylase activity (91.71 μmol/min). Among the nitrogen sources optimized,
peptone was found optimal for α-amylase production with activity of 90.34
μmol/min. pH 6.0 was found the best for the enzyme production. Effect of
incubation period on the enzyme production showed the 4th day of fermentation as
the peak day for α-amylase production from Aspergillus tamari. The results from
this study have shown that Aspergillus tamari among other fungal isolates from
mould bread collected from bakery sites in Enugu metropolis has the potential for
α-amylase production in a commercial scale for both industrial and clinical
applications.
Key words: 18s rDNA, α-amylase, fermentation, Optimization, Aspergillus tamarii T5
INTRODUCTION
α-amylase (1, 4-α-D-glucano hydrolase; E.C 3.2.1.1) is a ubiquitous enzyme responsible for
random hydrolysis of α 1-4, α1-6 glycosidic bonds in polysaccharides. Generally, the amylase
family (clan GH-H glycoside hydrolase) is the largest family of the glycoside hydrolase,
transferases and isomerases comprising nearly thirty different enzymes specificities
(Vijayaraghavan et al., 2011). As described by Vander Maarel et al. (2002) the family of the
amylase is categorized into four sub groups based on their specificity of their actions and they
include: endo, exo, debranching and transferase amylases. Verily α-amylase is widely
distributed in plants, animals and microbes, where they play important role of carbohydrate
metabolism (Swetha et al., 2006). Amylases from plants and animals suffer many demerits such
as: enzyme loads, doubling in production and ease of separations. Microbial amylases are
among the most important hydrolytic enzymes and have been studied extensively (Singh et al.,
2014). Their ease of separations, short doubling time and much know how technicality in
culturing and production makes much very indispensable for vast applications (clinical,
industrial and biotechnological bias fields). α- amylases have been reported to be produced by
a number of fungi including the family of Basidomycete, Ascomycete and the Deutromycetes
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European Journal of Applied Sciences (EJAS) Vol. 9, Issue 5, October-2021
Services for Science and Education – United Kingdom
(Balkan and Ertan, 2005, Nwagu and Okolo, 2011and Mohammed et al., 2007). Amylase family
represents one of the three largest groups of industrial enzymes and accounts for
approximately 25–33% of the world enzyme market (Van der maarel et al., 2002). They are
very indispensable in food industries necessarily for starch hydrolysis, clinical for replacement
therapy (case of metabolisms and in-born errors), chemical industries e.g detergent, pulp and
paper making etc (Mohammed et al., 2007). Search for novel strains of organisms with unique
ability for production of amylase has been of great paramount for much advanced
biotechnological relevance of the enzyme. Most applications of amylase occur at high
temperature and lower pH which are the conditions for starch hydrolysis and liquefaction.
((Goyal et al., 2005; Silva et al., 2005). Most α- amylases are seen denatured at these given
physiologic conditions and thus decreases their indispensability; however, novel strains of
filamentous fungi especially those of the basidomycetes and zygomycete families are of thermal
tolerant and can withstand relatively low pH condition. Production of α- amylases from these
organisms is believed to meet the desired condition required for industrial need of the enzyme.
The present study identifies some fungal strains using molecular techniques with unique
properties for production of α- amylases with promising enzymatic characteristics.
MATERIAL AND METHODS
All chemicals/reagents used in the present study are of analytical grade and are products of
Sigma-Aldrich, Bristol and May and baker. The analytical equipments are in good working
conditions and always calibrated at each use.
Sample Collection
Bread from bakery site was collected within the axis of Enugu metropolis in a clean plastic
container. Thereafter it was transported to the laboratory where it was placed in an anaerobic
jar for microbial infestations and decay.
Isolation and Identification of Fungal Strains from the Decayed Bread
Strains of fungi isolates were isolated from the decayed bread in a prepared nutrient broth
using standard microbiology (culturing and microscopy mounting) and biochemical (sugar
fermentations) techniques as described by Ezeonu et al.(2013).
Screening of Fungi isolates. for α-Amylase Production
Identified fungi isolates were screened for α-amylase producing ability using potato dextrose
broth supplemented with 2mM p-NPG as described by Gheytanchi et al. (2010). The inoculated
culture broth was incubated at 37°C for 3 days.
Molecular Identification of Aspergillus sp.
Genomic DNA (gDNA) from the selected isolate with high potentials of α-amylase production
was obtained using the QIA amp DNA Mini Kit. The 18S rDNA gene was amplified by RT-PCR
(the conditions for the amplification stated below) using the forward (5'-
GGTTTGATCATGGTCAG-3') and reverse (5'-AGTTACCTTGTTACGACT-3') primers. The
amplified DNA sequence was compared to the Gen Bank database of National Center for
Biotechnology Information (NCBI) using the BLAST program (Kumar et al., 2016).