10.7 Applications
223
also present in algae such as cyanobacterium (Singh et al. 2017). They are a diverse
group of proteins which include scytovirin, griffithsin and cyanovirin. Lectins have
the ability to bind to polysaccharides, glycans and glycolipids in a reversible manner
(Harnedy and FitzGerald 2011; Singh et al. 2015). This binding ability allows them
to cause cell agglutination and precipitation of glycoconjugates. This makes them
applicable in diverse applications such as antiviral, antitumor and antiinflammatory
agents and well as development of protein expression systems and nutraceuticals. The
use of lectins as microbicides to prevent the transmission of HIV has been explored
in several research studies (Janahi et al. 2018; Hopper et al. 2017; Alexandre et al.
2010). The lectins can selectively bind to the HIV cells by binding to the glycans
and polysaccharides on the surface of the virus which shields it from attack by the
antimicrobial agents or from being recognized by the body’s immune system. Lectins
also act by preventing the virus cells from binding to uninfected cells. This has been
demonstrated in in vitro studies on vaginal mucosa using scytovirin an algal lectin
(Janahi et al. 2018).
10.7.2 Phycobiliproteins
Phycobiliproteins are another form of proteins present in algae. These are watersoluble proteins that serve a role in capturing of light in photosynthesizing organisms. They are common in red algae and cyanobacteria (Dumay and Morancais
2016). Phycobiliproteins find commercial applications as natural dyes for food and
cosmetics (Spolaore et al. 2006). They also have been explored for other applications
such as fluorescent imaging and flow cytometry (Aneiros and Garateix 2004). More
recently, phycobiliproteins have been associated with some bioactive properties such
as antiviral, antiinflammatory and antioxidant activities (Sekar and Chandramohan
2008). Algae are also a source of certain bioactive polypeptides (Fan et al. 2014).
These have 2–30 repeating units of amino acids which have some bioactive properties
depending on the types and sequence of amino acids within these short chains. These
bioactive proteins are usually derived from the long-chain proteins and polypeptides
through hydrolysis or fermentation to break down the chains into shorter ones.
10.7.3 Food
Aquatic plant and algae play an increasingly important role in the future food security.
The world population is expected to reach 9 million by 2050, and the rate of food
production is being threatened due to several factors such as dangerous weather
conditions due to climate change and social problems leading to violence which has
resulted in reduced farming activities in these conflict regions (FAO et al. 2018).
There is an urgent need to develop alternative ways to produce food and produce it
much faster than conventional farming methods. With a much faster rate of nutrient
223
also present in algae such as cyanobacterium (Singh et al. 2017). They are a diverse
group of proteins which include scytovirin, griffithsin and cyanovirin. Lectins have
the ability to bind to polysaccharides, glycans and glycolipids in a reversible manner
(Harnedy and FitzGerald 2011; Singh et al. 2015). This binding ability allows them
to cause cell agglutination and precipitation of glycoconjugates. This makes them
applicable in diverse applications such as antiviral, antitumor and antiinflammatory
agents and well as development of protein expression systems and nutraceuticals. The
use of lectins as microbicides to prevent the transmission of HIV has been explored
in several research studies (Janahi et al. 2018; Hopper et al. 2017; Alexandre et al.
2010). The lectins can selectively bind to the HIV cells by binding to the glycans
and polysaccharides on the surface of the virus which shields it from attack by the
antimicrobial agents or from being recognized by the body’s immune system. Lectins
also act by preventing the virus cells from binding to uninfected cells. This has been
demonstrated in in vitro studies on vaginal mucosa using scytovirin an algal lectin
(Janahi et al. 2018).
10.7.2 Phycobiliproteins
Phycobiliproteins are another form of proteins present in algae. These are watersoluble proteins that serve a role in capturing of light in photosynthesizing organisms. They are common in red algae and cyanobacteria (Dumay and Morancais
2016). Phycobiliproteins find commercial applications as natural dyes for food and
cosmetics (Spolaore et al. 2006). They also have been explored for other applications
such as fluorescent imaging and flow cytometry (Aneiros and Garateix 2004). More
recently, phycobiliproteins have been associated with some bioactive properties such
as antiviral, antiinflammatory and antioxidant activities (Sekar and Chandramohan
2008). Algae are also a source of certain bioactive polypeptides (Fan et al. 2014).
These have 2–30 repeating units of amino acids which have some bioactive properties
depending on the types and sequence of amino acids within these short chains. These
bioactive proteins are usually derived from the long-chain proteins and polypeptides
through hydrolysis or fermentation to break down the chains into shorter ones.
10.7.3 Food
Aquatic plant and algae play an increasingly important role in the future food security.
The world population is expected to reach 9 million by 2050, and the rate of food
production is being threatened due to several factors such as dangerous weather
conditions due to climate change and social problems leading to violence which has
resulted in reduced farming activities in these conflict regions (FAO et al. 2018).
There is an urgent need to develop alternative ways to produce food and produce it
much faster than conventional farming methods. With a much faster rate of nutrient