Spirulina (Blue Green Algae) A Protein Treasure (70% of Protein)

Spirulina (Blue Green Algae) A Protein Treasure (70% of Protein)

 

Spirulina

Spirulina are multicellular and filamentous blue-green microalgae. Arthrospira platensis is the most common and widely available spirulina grows in water, can be harvested and processed easily and has significantly high macro- and micronutrient contents. It is used as human food as an important source of protein and is collected from natural water, dried and eaten.

        Spirulina is a primitive organism originating some 3.5 billion years ago that has established the ability to utilize carbon dioxide dissolved in seawater as a nutrient source for their reproduction. It is a photosynthesizing cyanophyte (blue-green algae) that grows vigorously in strong sunshine under high temperatures and highly alkaline conditions.

       In 1967 spirulina was established as a “wonderful future food source” in the International Association of Applied Microbiology (Sasson, 1997). Analysis of the nutritional properties of spirulina showed first and foremost an exceptionally high protein content, of the order of 60–70 percent of its dry weight; it also showed the excellent quality of its proteins (balanced essential amino acid content).

The spirulina Contains:

Protein: Spirulina contains unusually high amounts of protein, between 55 and 70 percent by dry weight, depending upon the source (Phang et al., 2000). It is a complete protein, containing all essential amino acids, though with reduced amounts of methionine, cystine, and lysine, as compared to standard proteins such as that from meat, eggs, or milk; it is, however, superior to all standard plant protein, such as that from legumes.

Essential fatty acids: Spirulina has a high amount of polyunsaturated fatty acids (PUFAs), 1.5–2.0 percent of 5–6 percent total lipid. In particular spirulina is rich in γ-linolenic acid (36 percent of total PUFAs), and also provides γ-linolenic acid (ALA), linoleic acid (LA, 36 percent of total ), stearidonic acid (SDA), eicosapentaenoic acid (EPA), docosahexaenoic acid (DHA) and arachidonic acid (AA). Spirulina has high quality protein content (59–65 percent), which is more than other commonly used Plant sources such as dry soybeans (35 percent), peanuts (25 percent) or grains (8–10 percent). A special value of spirulina is that it is readily digested due to the absence of cellulose in its cell walls.

Vitamins: Spirulina contains vitamin B1 (thiamine), B2 (riboflavin), B3 (nicotinamide), B6 (pyridoxine), B9 (folic acid), B12 (cyanocobalamin), vitamin C, vitamin D and vitamin E.

β-carotene: Spirulina contains large amounts of natural β-carotene and this β-carotene is converted into vitamin A. According to the findings of the National Cancer Institute, United States of America, an intake of 6.0 mg β-carotene daily may be effective in minimizing the risk of cancer.

Minerals: Spirulina is a rich source of potassium, and also contains calcium, chromium, copper, iron, magnesium, manganese, phosphorus, selenium, sodium and zinc.

Amino acids: Spirulina protein has a balanced composition of amino acids, with concentrations of methionine, tryptophan and other amino acids (Lysine, Phenylalanine, Tyrosine, Leucine, Glutamic acid, Aspartic acid, Cystine, Serine, Arginine, Histidine, Threonine, Proline, Valine, Isoleucine, Alanine and Glycine ) almost similar to those of casein.

Applications of Spirulina

Immune system enhancement: The Academy of Chinese Military Medical Sciences showed that spirulina could effectively improve the survival rate of mice after exposure to a lethal dose of radiation, prolong their survival time, and improve their immunity and activity of superoxide dismutase (SOD). Proved to be effective in lowering blood lipid, combating fatigue and increasing the level of immunoglobulin A (IgA) and immunoglobulin M (IgM). Phycocyanin of Spirulina platensis inhibits the growth of human leukemia K562 cells when supplemented with diet (Liu et al., 2000).

Nutritional supplement: Spirulina is rich in high quality protein, vitamins, minerals and many biologically active substances (Becker, 1994). Its cell wall consists of polysaccharide which has a digestibility of 86 percent, and could be easily absorbed by the human body. Spirulina is well known to have a very high iron content, it was tested against a typical iron supplement, iron sulfate. Spirulina-fed rats absorbed 60 percent more iron that rats fed the iron supplement. This study suggested that there is a highly assimilable form of iron in spirulina. A study also showed that it was effective in correcting anaemia in rats. A study showed the blood hemoglobin content increased from 10.9 to 13.2 (±21 percent) for human (female), a satisfactory level no longer considered anaemic (Henrikson, 1989). Spirulina significantly reduced the blood glucose level of both male and female.

Food source: when the algal cells or filaments of spirulina are transformed into powder it can provide the basis for a variety of food products, such as soups, sauces, pasta, snack foods, instant drinks and other recipes. Spirulina can be used as a partial supplementation or complete replacement for protein in aquafeeds.

Use as fertilizer:  blue-green algae replacing chemical fertilizers and rebuilding the structure of depleted soils (FAO, 1981)

Protein supplement in poultry and livestock feeds:

Fishmeal, groundnut meal and soybean meal can be partially replaced by spirulina in the preparation of diets of fish, poultry, cattle and domestic animals (Venkataraman, Somasekaran and Becker, 1994; El- Sayed, 1994; Britz, 1996).

Colorant in food products:

The blue-green colour of spirulina is due to two pigments: phycocyanin (blue) and chlorophyll (green). These two pigments are combined with another group of pigments known as carotenoids (red, orange and yellow). This phycocyanin extracted from spirulina was first marketed in 1980 by the Dainippon Ink & Chemicals Inc. under the brand name “Lina Blue-A”. This was mainly used as a food colourant, as an edible dye in ice creams and as a natural dye in the cosmetics industry. However, as the pigment was light sensitive, special care must be taken in protecting it from bleaching (Vonshak, 1990).

 REFERENCES

    Banerjee, M. & Deb, M. 1996. Potential of fly ash and Spirulina combination as a slow release fertilizer for rice field. Cientifica Jaboticabal, 24: 55–62.

    Becker, E.W. 1988. Microalgae for human and animal consumption. In M.A. Borowitzka & L.

    Borowitzka, eds. Micro-algal Biotechnology, pp. 222–256. Cambridge, Cambridge University Press.

    Becker, E.W. 1994. Microalgae. In Nutrition. pp. 196–249. Cambridge, Cambridge University Press.

    Belay, A., Yoshimichi, O., Miyakawa, K. & Shimamatsu, H. 1993. Current knowledge on potential health benefits of Spirulina. J. Appl. Phycol., 5: 235–241.

    M. Ahsan, B. Habib, Mashuda Parvin, FOOD AND AGRICULTURE ORGANIZATION OF THE UNITED NATIONS, Rome, 2008. A review on culture, production and use of spirulina as food for human and feed for domestic animal and fish.

Industrial Production of Beer

Industrial Production of Beer

Beer Production

Beer is a beverage containing alcohol, extract, and carbon dioxide. Beer is prepared from barley malt, raw hops or other hop products, brewing water, and top- or bottom-fermenting yeast. The alcohol must be produced exclusively from these ingredients, which are converted to fermentable products during the brewing process. The word beer comes from the Latin word ‘‘bibere’’ (to drink), which is the origin of the Old English word ‘‘be~or’’ (the brewed). The industrial production of beer process consist of various steps.

Milling

Beginning In the brew house, different types of malt (barley, corn, rice) are crushed together to break up the grain kernels in order to extract fermentable sugars to produce a milled product called grist.

Mash Conversion

The grist is then transferred into a mash tun and mixed with heated water in a process called mash conversion. The conversion process uses natural enzymes in the malt to break the malt’s starch down into sugars. Mashing allows the enzymes in the malt (primarily, α-amylase and β-amylase) to break down the starch in the grain into sugars, typically maltose to create a malty liquid called wort. The overall process will take up to 60-120 minutes.

Optimal rest temperatures for major mashing enzymes

 

Temp °C	Temp °F	Enzyme	Breaks down
40–45 °C	104.0–113.0 °F	β-Glucanase	β-Glucan
50–54 °C	122.0–129.2 °F	Protease	Protein
62–67 °C	143.6–152.6 °F	β-Amylase	Starch
71–72 °C	159.8–161.6 °F	α-Amylase	Starch

Lautering

The mash is then pumped into the lauter tun, where a sweet liquid (known as wort) is separated from the grain husks.

Boiling

The wort is then collected in a vessel called a kettle, where it is brought to a controlled boil before the hops are added. Hope are important as it gives characteristic flavour to the beer. Hops are a female flower of Humulus lupulus . Bitter and aroma imparting hops are used for brewing. They both differ in essential oil and alpha acid contents. Bitter hops are rich in alpha acid while aroma hops are rich in essential oils

Wort separation and cooling

After boiling, the wort is transferred into a whirlpool for the wort separation stage. During this stage, any malt or hop particles are removed to leave a liquid that is ready to be cooled, the WORT in a Plate Heat Exchanger from 100 °C to about 10 °C in an hour.

Fermentation

To start the fermentation, yeast is added during the filling of the vessel. Saccharomyces cerevisiae is used for beer manufacturing. Yeast converts the sugary wort into beer by producing alcohol, a wide range of flavors, and carbon dioxide. The cooled wort is transferred into a fermentation vessel to which the yeast has already added. If the beer being made is an ale, the wort will be maintained at a constant temperature of 20° C) for about two weeks. If the beer is a lager, the temperature will be maintained at (9-12°C) for about six weeks. Since fermentation produces a substantial amount of heat, the tanks must be cooled constantly to maintain the proper temperature. When fermentation has finished, the beer is cooled to about (0° C). This helps the remaining yeast settle to the bottom of the fermenter, along with other undesirable proteins that come out of solution at this lower temperature.

When the yeast first hits the wort, concentrations of glucose (C6H12O6) are very high, so through diffusion, glucose enters the yeast (in fact, it keeps entering the yeast as long as there is glucose in the solution). As each glucose molecule enters the yeast, it is broken down in a 10-step process called glycolysis. The product of glycolysis is two three-carbon sugars, called pyruvates, and some ATP (adenosine triphosphate), which supplies energy to the yeast and allows it to multiply. The two pyruvates are then converted by the yeast into carbon dioxide (CO2) and ethanol (CH3CH2OH, which is the alcohol in beer)

Maturation

After fermentation, the young “green” beer needs to be matured in order to allow both a full development of flavors and a smooth finish.

Filtration & carbonation

Now that most of the solids have settled to the bottom, the beer is slowly pumped from the fermenter and filtered to remove any remaining solids. From the filter, the beer goes into another tank, called a bright beer tank. This is its last stop before bottling or kegging. Here, the level of carbon dioxide is adjusted by bubbling a little extra CO2 into the beer through a porous stone. once completed, the beer is ready to be packaged

After filling the beer passed through pasteurizer before dispatch. 

Reference

Text Book of Microbiology : RC Dubey

Evan Evans (2011). The Oxford Companion to Beer. Oxford University Press. p. 236. ISBN 9780195367133. Archived from the original on 23 December 2019.

 Chris Boulton (20 May 2013). Encyclopaedia of Brewing. John Wiley & Sons. p. 111. ISBN 9781118598122. Archived from the original on 21 May 2016.

ChAd vaccine against Covid-19

ChAd vaccine against Covid-19

ChAd vaccine protects upper and lower respiratory tracts against SARS-CoV-2 (Covid-19)

Chimpanzee adenovirus vectors

Article Showed the researcher used ChAd vector as vaccine platforms for SARS-CoV-2. ChAd-SARS-CoV-2-S encodes for SARS CoV-2 S protein with the two indicated proline mutations. Single dose immunization of a stabilized S protein-based vaccine via an intramuscular route induced S- and RBD-specific binding as well as neutralizing antibodies. Vaccination with one or two doses protected mice expressing human ACE2 against SARS-CoV-2 challenge, as evidenced by an absence of infectious virus in the lungs and substantially reduced viral RNA levels in lungs and other organs.

Immunization with ChAd-SARS-CoV-2-S induces both neutralizing antibody and antigen-specific CD8+ T cell responses. While a single intramuscular immunization of ChAd-SARS-CoV-2-S confers protection against SARS-CoV-2 infection and inflammation in the lungs, intranasal delivery of the vaccine induces mucosal immunity, provides superior protection, and possibly promotes sterilizing immunity, at least in mice that transiently or stably express the hACE2 receptor. Image credit: Hassan et al, doi: 10.1016/j.cell.2020.08.026.

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a positive-sense single-stranded RNA virus that was first isolated in late 2019 from patients with severe respiratory illness in Wuhan, China. SARS-CoV-2 is related to two other highly pathogenic respiratory viruses, SARS-CoV and Middle East respiratory syndrome coronavirus (MERS-CoV). SARS-CoV-2 infection results in a clinical syndrome, Coronavirus Disease 2019 (COVID-19) that can progress to respiratory failure and also present with cardiac pathology, gastrointestinal disease, coagulopathy, and a hyperinflammatory syndrome.

    Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)    

        The SARS-CoV-2 RNA genome is approximately 30,000 nucleotides in length. The 5’ two-thirds encode nonstructural proteins that enable genome replication and viral RNA synthesis. The remaining one-third encode structural proteins such as spike (S), envelope, membrane, and nucleoprotein (NP) that form the spherical virion, and accessory proteins that regulate cellular responses. The S protein forms homotrimeric spikes on the virion and engages the cell-surface receptor angiotensin-converting enzyme 2 (ACE2) to promote coronavirus entry into human cells.

        The SARS-CoV and SARS-CoV-2 S proteins are cleaved sequentially during the entry process to yield S1 and S2 fragments, followed by further processing of S2 to yield a smaller S2' protein. The S1 protein includes the receptor binding domain (RBD) and the S2 protein promotes membrane fusion.This form of the S protein is recognized by potently neutralizing monoclonal antibodies and could serve as a promising vaccine target. Single intranasal dose of ChAd-SARS-CoV-2-S induced high levels of neutralizing antibody and anti-SARS-CoV-2 IgA, and conferred virtually complete protection against infection in both the upper and lower respiratory tracts in mice expressing hACE2 receptor after adenoviral vector delivery or as a trans gene. It has the potential to control infection at the site of inoculation, which should prevent both virus-induced disease and transmission.

Immunogenicity of ChAd-SARS-CoV-2-S, groups of 4-week-old BALB/c mice were immunized by intramuscular inoculation with 10¹⁰ virus particles of ChAd-SARS-CoV 2-S or ChAd-control. Some mice received a booster dose four weeks later. Serum samples were collected 21 days after primary or booster immunization, and IgG responses against purified S and RBD proteins were evaluated by ELISA. Whereas ChAd-SARS-CoV-2-S induced high levels of S- and RBD-specific IgG, low levels were detected in the ChAd control-immunized mice.

Vaccine-induced memory CD8+ T cell and antigen specific B cell responses.

Intramuscular immunization with ChAd-SARS-CoV-2-S vaccine protects against               SARS- CoV-2 infection in the lung.

A single intranasal immunization with ChAd-SARS-CoV-2-S prevents SARS-CoV-2 infection in the upper and lower respiratory tracts of hACE2 transgenic mice. Recently established a more stringent, lethal SARS-CoV-2 challenge model in transgenic C57BL/6 mice that have eight inserted copies of the hACE2 gene driven by the K18 cytokeratin epithelial cell promoter. Within one week of SARS-CoV-2 inoculation by an intranasal route, K18- hACE2 mice develop severe lung infection and inflammation, immune cell infiltration, and compromised respiratory function that results in death. As an independent test of the efficacy of intranasal administration of ChAd-SARS-CoV-2-S, Researcher assessed its immunogenicity and protective efficacy in K18-hACE2 mice. Four-week old K18-hACE2 mice were inoculated via an intranasal route with 10¹⁰ viral particles of ChAd-control or ChAd-SARS-CoV-2-S. Serum samples were collected at four weeks post-immunization and humoral immune responses were evaluated. Intranasal immunization of ChAd-SARS-CoV-2-S but not ChAd-control induced high levels of S- and RBD specific IgG and IgA and neutralizing antibodies (GMT of 1/1,424) in serum. At day 30 post-vaccination, K18-hACE2 mice were challenged via an intranasal route with 10³ FFU of SARS-CoV-2. At 4 dpi, lungs, spleen, heart, nasal turbinates, and nasal washes were harvested and assessed for viral burden. Similar to that seen in BALB/c mice transiently expressing hACE2, intranasal immunization of ChAd-SARS-CoV-2-S conferred remarkable protection as judged by an absence of infectious virus in the lungs, no measurable viral  subgenomic/genomic RNA in the lungs or hearts, and very low levels of viral RNA in the nasal  turbinates or washes. Consistent with these results, after SARS-CoV-2 challenge, observed no induction of cytokine and chemokine mRNA (e.g., CCL2, CXCL1, CXCL10, 297 CXCL11, IL6, IFNβ, and IFNλ) in the lung homogenates of ChAd-SARS-CoV-2-S-immunized  compared to naïve mice, whereas ChAd-control vaccinated mice sustained high levels . Collectively, these data suggest that a single intranasal immunization of ChAd-SARS-CoV-2-S induces robust systemic and mucosal immunity that blocks SARS-CoV-2 infection in the upper and lower respiratory tract of highly susceptible K18-hACE2 transgenic mice, source from article.

Reference

A.O. Hassan et al. 2020. A single-dose intranasal ChAd vaccine protects upper and lower respiratory tracts against SARS-CoV-2. Cell, in press; doi: 10.1016/j.cell.2020.08.026