Among the many different types of enzymes available, Cellulase is produced by several different bacteria, fungi, and other carbon sources. These bacteria are used to produce Cellulase enzymes for a variety of industrial applications, from biodegradable plastics to biofuels. While these bacteria are essentially the same, some may have specific advantages over others. For example, some have better enzyme activity and superior enzymatic activity.
The purification process of the cellulase enzyme was performed using the CMC column chromatography method. Cellulase had a total activity of 81,788 U/L. The yield was 35.7%, and the molecular weight of the enzyme was found to be 67 kDa. The deduced amino acid sequence was then subjected to a BLASTP search using the NCBI database61. The results showed that the cellulase enzyme encoding ORF had a high specificity toward CMC.
To evaluate the effects of temperature on cellulase activity, Bacillus cereus was grown at different temperatures. Maximum cellulase activity was obtained at 35 degC. Enzyme activity decreased as the temperature was raised. On the other hand, the cellulase enzyme from Bacillus pumilis showed higher activity at 35 degC. Moreover, it was able to degrade cellulose with greater efficiency compared to Bacillus cereus.
In addition to promoting improved digestion, Cellulase also has industrial uses. Its production increases the availability of nutrient-rich whole grains. However, the benefits of cellulase enzymes have not been studied in vivo. One recent study showed that patients in a nursing home ingested a multi-enzyme formula. This improved digestion should translate to improved health. Although these results were short-lived, the improved immune function was evident once the supplement was stopped.
Cellulase Enzyme production
During the cellulase enzyme production process, a growth curve of endo-(1,4)-b-D-glucanase is used to estimate the optimum time for the production process. The graphs below show the growth curve and cellulase activity for each enzyme. The graphs show the maximum cellulase activity, lowest cellulase activity, and lowest endo-(1,4)-b-D-glucanase activity on a substrate with a high ratio of enzymes to cellulose.
The microbial strains used in cellulase enzyme production are selected based on their properties. A fungus, Trichoderma reesei RUT C30, is one such fungus. Researchers focused on this strain because of its availability, high cellulase activity, and lower cost. The fungus has been used to produce a wide range of cellulases.
In addition to Parthenium hysterophorus, a weed used in bioreactors is a suitable cellulase substrate. Optimization studies showed that the optimal growth conditions for T. reesei for cellulase production were 30 degC, 8 days, and a 1:2 initial solid-to-liquid ratio. For optimal CMCase and FPase production, the optimal inoculum age was 120 h.
Cellulase producing bacteria
Many microorganisms produce cellulases when grown on cellulolytic substrates, such as cellulose or wood pulp. Among these microorganisms, bacterial cellulases have several advantages over other kinds of enzymes, including high productivity, easy recovery, and resistance to extreme environmental conditions. Bacillus subtilis, for example, is a notable working house for lytic enzymes and has an enzymatic activity that varies significantly with different environmental conditions.
The production of cellulase enzymes results from microbial growth, which results in a variety of industrial applications. Bacillus subtilis, bacillus lichen forms, bacillus cereus, and azobacter were isolated from the Florida Everglades’ flora. Other bacterial isolates did not show clear zones in the control plate, so they were not considered cellulase-producing bacteria.
Bacteria that produce Cellulase can degrade cellulose into glucose. This process is possible because cellulose is present in vast quantities in the earth’s environment. This unbranched polymer contains glucose monomers linked by b-1,4 glycosidic bonds, making it resistant to hydrolysis. Therefore, the production of cellulase enzymes is crucial to harnessing the energy present in cellulose.
Cellulose and Cellulase
The cellulase enzyme is an important industrial enzyme that catalyzes the degradation of cellulose and related polysaccharides. Bacteria, fungi, and protozoans produce cellulases. They are used for a wide range of applications in food processing and in the non-food industry. Cellulases are also used in pharmaceutical research. In this article, we’ll discuss the role of cellulases in our lives.
Various enzymes are used to treat cellulose, and cellulase activity is one of them. Cellulase enzymes have three groups and act on cellulose to break down the b1-4 linkages. Repeated washing and usage of cellulose fibers damage the fibers. By digesting the fiber, cellulase enzymes make fabrics and yarns more attractive and durable. Enzymes used in detergents are highly stable in alkaline conditions, making them suitable for use as additives in laundry detergents.
Studies on cellulase enzymes have resulted in significant scientific knowledge and unlocked the enormous potential in biotechnology. Cellulase enzymes break down biomass and convert it to fuel ethanol, a clean alternative to fossil fuels. Cellulase enzyme technology is currently available for industrial scale-up. This review will give an overview of the technology and highlight its most promising prospects.
Isolation and characterization of Cellulase
The optimum growth conditions and carbon and nitrogen sources for cellulase enzyme production from a microbial source are vital for maximum yields. Furthermore, further studies must be performed to purify and clone microbial cellulases for use in industry. Moreover, a new enzyme can be engineered using random mutagenesis and rational design techniques.
After purification, enzyme activity was measured using standard assay conditions and metal ions. The enzymes were incubated in different organic solvents, and the residual activity was calculated against the control solvent. The activity was stable at optimum pH and temperature for more than 8 hours. Similarly, cellulase activity was not affected by end-product inhibition, which was found in the presence of glucose and cellobiose.
Purified cellulose was purified by a process described by Ibraheem et al. (2017). The cellulose was precipitated by adding 80 % ammonium sulphate. Then, the precipitate was centrifuged at 10,000 x g for 30 min. After further decantation of the supernatant, the partially purified Cellulase was poured into a dialysis tube.
Cellulase enzyme in the human body
The Cellulase enzyme is helpful to the human body as it breaks down cellulose into beta-glucose, which the body can use for various purposes. Cellulases also help regulate blood sugar levels and eliminate harmful organisms from cell membranes. It is an important component of many foods and beverages and is widely used in the textile and laundry detergent industry. They are also used in biofuel fermentation and the production of paper.
The human body does not naturally produce Cellulase, so scientists must rely on other sources for this important enzyme. Luckily, cellulase enzymes are found in plants and can be bought at most grocery stores. There are several kinds of cellulase enzymes. The endocellulase breaks down cellulose, while the exocellulase depolymers the ends into a maximum of four units.
Cellulases catalyze reactions by interacting with a single polysaccharide strand, called the o-glycosidic bond. Non-progressive cellulases disengage from the polysaccharide, which causes a high blank value in traditional reducing sugar assays. The inverting/retaining mechanism of cellulases results from the presence of several enzymes with wide-ranging substrate specificities.
Function of Cellulase
The function of the cellulase enzyme is to digest cellulose fibers to produce a softer, more pliable fabric. It acts on cellulose polymers by cleaving their b1-4 linkages. It is an important enzyme in the textile industry because of washing and usage damage cellulose fibers. Cellulase enzymes are also used in detergents to increase the finishing of fabrics and yarn.
The enzyme’s action mechanism depends on the distance between its catalytic sites. The distance between these sites determines the specific type of cellulase enzyme. Both processive and non processive cellulases release reducing sugars in the substrate. Both types of enzymes are nucleophilic. The enzyme’s activity is measured by the amount of water the substrate can absorb during a minute-long reaction.
To produce cellulase enzymes, microbial strains have been studied extensively. Cellulolytic enzymes can be produced from different waste feedstocks. Various genetic manipulations can enhance yield, efficiency, specificity, and cost-efficiency. Furthermore, microbial co-production of essential molecules can boost the cost-efficiency of cellulase production. This can help industrialists produce a high-quality enzyme at a reasonable price in the long run.