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J. A. Elegbede and A. Lateef
for modification of product and optimization owing to the openness to gene manipulation, and biochemical diversity in microorganisms. The process of enzyme production can be improved by engineering techniques and the characteristics of enzymes
can be altered by protein engineering (Gurung et al. 2013). Moreover, microbes
represent a plenteous source for the novel microbial enzymes discovery via contemporary methods such as genome mining, metagenome screening and investigating
the biodiversity of extremophiles (Sabu 2003; Adrio and Demain 2014).
Microbial enzymes are widely employed in diverse sectors including food, agriculture, medicine, chemicals and energy (Singh et al. 2016). Moreover, protein
engineering and DNA recombinant techniques have made exploitation of microbial
strains achievable in meeting the ever-rising need for enzymes with novel characteristics (Liu et al. 2015). Furthermore, the microorganism exhibits metabolic dynamism,
ease of large scale cultivation by fermentation, need of non-complex nutrients and
is unaffected by seasonal conditions (Sharma and Upadhyay 2020). It will be true
to assume the impracticability of any biological process with no enzymes. Enzymes
are biocatalysts, which boost the reaction speed to several folds. All enzymes are
protein in nature excluding catalytic RNA molecules, and all are required for all
living organisms. Usually, the catalytic activity of enzymes results from the integrity
of protein conformation and this is lost if the enzyme is denatured. The active or
functional site of enzymes is the specific site which is the area of connection of the
enzyme to its specific substrate to produce the product. Typically, the functional site
is cleft or groove on the surface of enzyme that creates a non-polar environment that
helps in proficient attachment to a substrate (Sharma and Upadhyay 2020).
Enzymes are comprised of several amino acid molecules with each residue of
amino acid covalently joined to its neighbor; the amide linkage between them is
described as a peptide bond. They are large macromolecules ranging between kilodaltons to megadaltons in terms of molecular mass (Singh et al. 2016). Generally,
enzymes contain 20 different amino acids types, and depending on the kind of reaction they facilitate, according to the International Union of Biochemistry (IUB), they
can be grouped into six classes: hydrolases, transferases, lyases, isomerases, oxidoreductases and ligases (Sanchez and Demain 2017). Currently, according to Li et al.
(2012), just about two hundred (200) kinds of enzymes from microbial resources of
about four thousand (4000) recognized enzymes are commercially applied and just
about twenty (20) are produced on an actual industrial scale.
2.2 Production of Microbial Enzymes
Enzyme production is a field that is very important in biotechnology (Couto and
Sanromán 2005). Lignocellulosic biomass is utilized as a low-cost raw material
which is used for cost-effective manufacture of enzymes as a result of their cheap
commercial value. The application of lignocellulosic resources in enzymes production has resulted in decrease in environmental pollution caused by the unfavorable
production of massive amounts of lignocellulosic resources. Microbes (fungi and
J. A. Elegbede and A. Lateef
for modification of product and optimization owing to the openness to gene manipulation, and biochemical diversity in microorganisms. The process of enzyme production can be improved by engineering techniques and the characteristics of enzymes
can be altered by protein engineering (Gurung et al. 2013). Moreover, microbes
represent a plenteous source for the novel microbial enzymes discovery via contemporary methods such as genome mining, metagenome screening and investigating
the biodiversity of extremophiles (Sabu 2003; Adrio and Demain 2014).
Microbial enzymes are widely employed in diverse sectors including food, agriculture, medicine, chemicals and energy (Singh et al. 2016). Moreover, protein
engineering and DNA recombinant techniques have made exploitation of microbial
strains achievable in meeting the ever-rising need for enzymes with novel characteristics (Liu et al. 2015). Furthermore, the microorganism exhibits metabolic dynamism,
ease of large scale cultivation by fermentation, need of non-complex nutrients and
is unaffected by seasonal conditions (Sharma and Upadhyay 2020). It will be true
to assume the impracticability of any biological process with no enzymes. Enzymes
are biocatalysts, which boost the reaction speed to several folds. All enzymes are
protein in nature excluding catalytic RNA molecules, and all are required for all
living organisms. Usually, the catalytic activity of enzymes results from the integrity
of protein conformation and this is lost if the enzyme is denatured. The active or
functional site of enzymes is the specific site which is the area of connection of the
enzyme to its specific substrate to produce the product. Typically, the functional site
is cleft or groove on the surface of enzyme that creates a non-polar environment that
helps in proficient attachment to a substrate (Sharma and Upadhyay 2020).
Enzymes are comprised of several amino acid molecules with each residue of
amino acid covalently joined to its neighbor; the amide linkage between them is
described as a peptide bond. They are large macromolecules ranging between kilodaltons to megadaltons in terms of molecular mass (Singh et al. 2016). Generally,
enzymes contain 20 different amino acids types, and depending on the kind of reaction they facilitate, according to the International Union of Biochemistry (IUB), they
can be grouped into six classes: hydrolases, transferases, lyases, isomerases, oxidoreductases and ligases (Sanchez and Demain 2017). Currently, according to Li et al.
(2012), just about two hundred (200) kinds of enzymes from microbial resources of
about four thousand (4000) recognized enzymes are commercially applied and just
about twenty (20) are produced on an actual industrial scale.
2.2 Production of Microbial Enzymes
Enzyme production is a field that is very important in biotechnology (Couto and
Sanromán 2005). Lignocellulosic biomass is utilized as a low-cost raw material
which is used for cost-effective manufacture of enzymes as a result of their cheap
commercial value. The application of lignocellulosic resources in enzymes production has resulted in decrease in environmental pollution caused by the unfavorable
production of massive amounts of lignocellulosic resources. Microbes (fungi and