INTRODUCTION:

Enzymes are proteins that control the speed of chemical reactions in your body. Without enzyme, these reactions would take place too slowly to keep you alive. Enzymes are globular shaped proteins that are found throughout the body, with their main function being to act as biological catalysts. An enzyme can act to speed up or regulate the rate of the reaction in order to maintain an efficient rate of biological reaction. Enzyme plays important role in the reaction of many chemicals within the body, are not consumed in the reaction and so are able to catalyze many reaction in their life cycle.) Enzymes are able to reduce the activation energy of the reaction, the energy required to break bonds between the reactants, and form new bonds in the products, which allows more product to be formed¹.

Enzymes enable the reaction to take place more rapidly at a safer, relatively low temperature that is consistent with living systems. During an enzyme-mediated reaction, the substrate physically attaches to the enzyme at its active site, allowing the substrate (s) to be converted to new product molecule (s). Most enzyme reaction rates are millions of times faster than those of comparable uncatalyzed reactions.

Enzymes are neither consumed by the reactions they catalyze, nor do they alter the equilibrium of these reactions. Enzymes are known to catalyze about 4,000 biochemical reactions².

In 1876, William Kuhne proposed that the name 'enzyme' be used as the new term to denote phenomenon previously known as 'unorganized ferments', that is, ferments isolated from the viable organisms in which they were formed. The word itself means 'in yeast' and is derived from the Greek 'an' meaning 'in', and 'zyme' meaning 'yeast' or 'leaven'. This important achievement was the first indication that enzymes could function independently of the cell. It was not until 1926, however, that the first enzyme was obtained in pure form, a feat accomplished by American biochemist James B. Sumner of Cornell University. Sumner was able to isolate and crystallize the enzyme urease from the jack bean. His work was to earn him the 1947 Nobel Prize. John H. Northrop and Wendell M. Stanley of the Rockefeller Institute for Medical Research shared the 1947 Nobel Prize with Sumner³.

A complex procedure for isolating pepsin was devised by Northrop and Stanley has been used to crystallize several enzymes⁴. Enzymes are proteins and are nature’s own biocatalyst and their function is determined by their complex structure. With the exception of a small group of catalytic RNA molecules, all enzymes are proteins which are made up of amino acids linked together by peptide bonds⁵.

Pectin lyases:

Pectin is a structural heteropolysaccgaride contained in the primary cell walls of terrestrial plants. It was first isolated and described in 1825 by Henri Braconnot. Pectin lyase are the only known pectinase capable of degrading highly esterifies pectin’s(like those found in fruits) into small molecules via B-elimination mechanism without producing methanol, in contrast with the combination of polygalacturonase and pectin esterase, which are normally found in commercial products. Today, the application of pectinolytic enzymes plays an important concentration role in food technology for the maceration of fruits and vegetables, as well as for the extraction, concentration and clarification of their juices. For this purpose, the selection of carbon source and nitrogen source with low value is a practical consideration. Many waste products from the agricultural industry containing pectin, such as sugar beet pulp(SBP),citrus pulp pellets, apple, pumice, henequen pulp, lemon pulp and other related materials have been used as carbon source for induction of pectinase by many microorganisms. Several agro-industrial and by-products such as orange bagasse, sugar cane bagasse, and other food processing waste are effective substrates for de-polymerizing enzyme production by solid state fermentation. Recently, a large number of microorganisms, isolated from different materials, have been screened for their ability to degrade polysaccharide present in vegetable biomass producing pectinase on solid state culture as shown in Fig.1. In light of the above points, the aim of this work was to study of polygalacturonase enzyme production by isolated strains of fungi by solid state fermentation using agro industrial by products. The alkaline pectinase is inappropriate for use in the food industry due to the acidic pH of fruit juices. However, they have a very high demand in the textile industries. They are used for retting of plant fibers such as ramie, sun hemp, jute, flax and hemp. The first report on retting of sun hemp (Crotalaria juncea) by pectin lyses produced by Aspergillus flavus (MTCC 7589) was published in 2008⁶.

Many plant-pathogenic bacteria and fungi are known to produce pectinolytic enzymes useful for invading host tissues. Moreover, theses enzyme are essential in the decay of dead plant material by nonpathogenic microorganisms and thus assist in recycling carbon compounds in the biosphere.

Cellulase:

Cellulases are a group of hydrolytic enzymes which are capable of depolymerizing cellulose to smaller molecules⁷. These enzymes are produced mainly by fungi though some bacterial strains have also been found to produce cellulase. The production of cellulase has been reported from a wide variety of bacteria.

The third but the most significant group of lignocellulolytic enzyme is cellulase the key enzymes for the conversion of cellulose into simple sugars⁸. Cellulase is a family of enzymes hydrolysing beta -1,4- glycosidic bonds of intact cellulose and other related celloligosaccharide derivatives synergistic action of three principal types of the enzymes, viz, endoglucanase (EC 3.2.1.4), exoglucanase (EC 3.2.1.91) and fungi are preferred for commercial enzyme production, because the level of the enzymes produced by these cultures is higher than those obtained from yeast and bacteria. Almost all fungi of genus Aspergillus synthesize cellulase, therefore this genus has the enzyme industry. Aspergillus and Trichoderma spp. are well known efficient production of cellulases⁹.

Cellulases are enzymes which catalyze the hydrolytic degradation of cellulosic biomass¹⁰. These enzymes can be obtained from microorganisms grown on cheap agro-industrial materials. Cellulases are divided into three major groups Endoglucanase, which randomly attacks the internal beta-1, 4- glycosidic bonds, resulting in glycan chains of different lengths. Exoglucanases or cellebiohydrolases acts on reducing ends of the cellulose chain and releases beta- cellobiose as the end product. Beta- Glucosidase acts specifically on the beta-cellobiose disaccharides and produce glucose¹¹.

Cellulase are the enzymes that hydrolyze beta-1, 4 linkages in cellulose chains. They are produced by fungi, bacteria, protozoans, plants, and animals. The catalytic modules of cellulases have been classified into numerous families based on their amino acid sequences and crystal structures¹². Due to their importance in saccharification, cellulases are widely using in food bewarages, wine, animal feed, textile and laundry, paper and pulp industries as well as in agriculture and for research purpose.

Cellulases are the ubiquitous enzymes that catalyze hydrolysis of the beta-1, 4-linkage, which joins two glucose molecules in a cellulose chain. Each of them from discrete units called domains. Cellulases are unique in a way that they degrade an insoluble substrate by diffusing in the substrate and then transport a segment of a cellulose molecule into its active site, thereby causing its degradation.

SOURCE:

The word fungus comes from the Latin word from mushrooms. Indeed, the familiar mushroom is a reproductive structure used by many type of fungi. However, there are also many fungi species that don`t produce mushrooms at all. Being eukaryotes, a typical fungal cell contains a true nucleus and many membrane-bound organelles. The kingdom fungi include an enormous variety of living organisms collectively referred to as Ascomycota, or true fungi. While scientists have identified about 100,000 species of fungi, this is only a fraction of the 1.5 million species of fungus probably present on earth. Edible mushrooms, yeasts, black mold and the producer of the antibiotic penicillin, Penicillium notatum, are all members of the kingdom fungi, which belongs to the domain Eukarya.

Fungi produce several extracellular enzymes that result in the decomposition of organic matter and one such enzyme is pectinolytic enzymes. The fungus produces these enzymes to break down the middle lamella in plants so that it can extract nutrients from the plant tissues and insert fungal hyphae. The members of the fungal genus Aspergillus niger are commonly used for the production of polysaccharide degrading enzymes shown in Fig.1 This genus produces a wide spectrum of cell wall degrading enzymes, allowing not only complete degradation of the polysaccharide but also tailored modification by using specific enzymes purified from these fungi. In this study an attempt has been made to isolate and screen fungi from different sources for their ability to produce pectinolytic enzymes.

Fungi are also used for the production of fermented food and beverages in all traditional and indigenous cultures in the world. Examples include cheeses, bread, beer, wine, cider, rice and soy sauce. Humans have exploited the natural abilities of fungi to ferment fruits and grains to produce alcoholic beverages and bread since as early as 6000 BCE and for cheese since at least 7500 BCE. Yeasts are used for the fermentation of bread, wine and beer, while filamentous fungi are used for the maturation of cheese and soy sauces.

Since ancient times, humans have used fungi as food sources. The edible sexual structures of Basidiomycetes (e.g., truffles), the so-called mushrooms, are produced mostly in wood because many fungi are three symbiosis or decoyers of tree tissues. These fruiting bodies represent a rich source of proteins, with low fat content and otherwise nutritionally quite poor. Humans have used Saccharomyces yeasts for thousands of years of brewing, baking and wine making. Because yeasts are able to convert sugars into alcohol, they were used primarily as effective ways to preserve the quality and safety of foods and beverages, because high contraptions of ethanol or toxic for most other microbes.

Today, more than 200 wine strains of S. cerevisiae are used to inoculate grape musts. These strains have been selected from spontaneous fermentations or selected in the vineyard environments according to particular fermentative capacities, tolerance to stresses particularly ethanol and sulfites, and the limited production of undesirable compounds such as H₂S and acetate.

Rice bran act as an animal food because it’s high cellulose content. It does not find any significant commercial application till now and most of this byproduct is generally disposed of in open areas, leading to serious environmental problems. Given this situation, it is necessary to look for processes that allow the controlled elimination of this residue or even better its industrial reutilization. Plant cell walls are the most abundant renewable source of fermentable sugars on earth

The environmental crisis which the world is experiencing forces us to re -evaluate the efficient utilization or finding alternative uses for natural renewable resources especially organic waste. Lignocellulose in the form of cellulose which is the most important renewable sources in the biosphere have been shown to be used in the production of valuable products by microorganisms specially fungi. The effects of five different mangrove fungi were evaluated on the extent of cellulolytic enzyme production. H₂SO₄ pretreated sawdust was found to be a good source for enzyme production.

The effect of different carbon sources namely, rice straw, wheat straw, wheat bran, bagasse, corncob, saw dust, sorghum straw and paper on the production of endoglucanase, β-glucosidase, Fpase and xylanase was studied.

The effect of organic (peptone, malt extract, beef extract, tryptone, yeast extract, urea, soya bean meal, corn steep liquor) and inorganic (NH₄Cl, NH₄NO₃, (NH₄)2HPO₄, ammonium acetate) nitrogen sources on the production of endoglucanase, β glucosidase, Fpase and xylanase was studied by replacing ammonium acetate.

APPLICATION:

Pectinase are enzymes with catalyze the hydrolysis of glycoside bonds in pectin polymers. Pectin substances found in tomato, pineapple, orange, apple, lemon pulp, orange peel and other citrus fruits act as natural substrate for this enzyme. Functionally pectinase can be categorized as polygalacturonases (which hydrolyze glycoside α-(14) bonds), pectin esterase’s (which remove acetyl and methoxyl groups from pectin), pectin lyase and pectate lyase. Pectinase can be produced from natural as well as recombinant microbes with attempts made to increase their thermo stability and yield. Pectinase can also act their own smooth or hairy regions of pectin. Based on pH, there are acidic and alkaline Pectinase also grouped in endo-pectinase when enzyme cleaves randomly and exopectinase when the terminal ends are targated.

Pectinase find a multitude of industrial applications such as in paper bleaching, food industry, remediation, etc. Juices with added pectinase have a clearer appearance and filterability than enzyme depleted counterparts. Apart from reducing the turbidity and haze generation of naturally derived fruit juices such as apple and banana. Pectinase also improve the color and flavor of drinks. The addition of gelatin and pectin greatly increases the viscosity and turbidity of juices and removal of the haze is the most costly part of juices production. The use of biogenic enzymes such as pectinase in juices would act almost nine times better than mechanical maceration to get good results.

Pectinase production occupies about 10% of the overall manufacturing of enzyme preparations. These enzymes are widely used in the food industry in the production of juices, fruit drinks and wines.

Acid pectinase, which are widely used in extraction, clarification and removal of pectin in fruit juices, in maceration of vegetables to produce pastes and purees, and in wine-making, are often produced by fungi, especially Aspergillus niger.

The crushing of pectin-rich fruits results in high viscosity juice which stays linked to the fruit pulp in a gelatinous structure, hindering the juice extraction process by pressing. Pectinase addition in the extraction process improves the fruit juice yield through an easier process, decreases the juice viscosity and degrades the gel structure, thus improving the juice concentration capacity. In the case of fruit juice, extraction by enzymatic maceration can increase yields by more than 90% compared to conventional mechanical juicing, besides improving the organoleptic (colour, flavor) and nutritional (vitamins) properties and technological efficiency (ease of filtering).

In several processes, enzymes are applied associated with other cell wall degrading enzyme pectinolytic such as cellulase and hemicellulase. The mixture of pectinase and cellulase has been reported to improve more than 100 % juice extraction yields. Sources and coworkers reported an improvement between three and four times in juice yields from papaya, banana and pear using enzyme extraction instead of the conventional pressing process.

The enzyme treatment can help decrease 62 % of the apple juice viscosity. When the depectinized apple juice is ultra filtered, the permeate flux is much higher than when undepectinized juice in processed. The increase in the permeation rate is a result of both the reduction in apple juice viscosity and the reduction in total pectin content. Pectin is a fiber shaped colloid that causes severe fouling of ultra filtration membranes.

The commercially available pectinase preparations used in food processing are traditionally associations of polygalacturonase, pectin lyases and pectin methyl esterase’s. These preparations are usually derived from fungi, mainly the genera Aspergillus.

Alkaline pectinase are generally produced by bacteria, particularly species of bacillus, but are also made by some filamentous fungi and yeasts. They may be used in the pretreatment of waste water from vegetable food processing that contains pectin residues; the processing of vegetable oil extraction and the treatment of paper pulp. Pectinolytic enzymes have been applied to the degumming of jute, sun hemp, flax, and Ramie and coconut fibers for textile application.

Cellulases are used in the textile industry in detergents, pulp and paper industry, improving digestibility of animal feeds, and food industry. They account for a significant fraction of industrial enzyme markets. Cellulase market will grow rapidly. For example, if the goal of the department of energy that the production of 45 billion gallon of cellulosic ethanol in 2030 comes true with an assumption of cellulase cost ($0.20 dollar per gallon) the projected yearly cellulase market will be as large as 9 billion dollars. Obviously, cellulase will be the largest industrial enzyme as compared to the current market size for all industrial enzymes ($~2 billion).

Currently intensive research has been carried out for the production of clean and sustainable energy source from renewable carbon sources as a possible alternative of fossil fuels. Bio production of hydrogen by fermentation of cellulosic material is considered as a clean and renewable energy source. Consumption of reducing sugar by non-cellulolytic microorganism in fermentation process limits hydrogen production. However, enzymatic hydrolysis of cellulosic material by cellulases followed by subsequent hydrogen production from hydrolysates using hydrogen producers offers economically feasible and low energy demanding method with maximum energy yield.

Cellulases are widely used in the textile industry for stone- washing of denim garments and to remove pills and fuzz fibers for softening and improving fabric look. Additionally, they also serve as detergents and enhance color brightness and clean fiber surfaces. Low rate of enzymatic degradation of fabric increases fiber properties without causing intensive damage¹³. Cellulases help in improving and maintaining the stability of soils by releasing nutrients such as nitrogen and phosphorous through mineralization of organic matte¹⁴. Moreover, cellulases increase microbial activity and also buffer the pH of soils thereby promoting plant growth. Cellulases are known to be effective biocontrol agent against pathogenic oomycetes, Pythium ultimum and phytophthora parasitic.

In food industry, cellulases are used for extraction and clarification of vegetable and fruit juices by maceration the pulp to liquefaction, thereby increasing juice yield. They are also involved in extraction olive oil and production of fruit nectars and purees. They increase nutritional value of monogastric feeding by reducing anti-nutritional factors in grains and vegetable. Therefore, growing demand of cellulases in food industry has steered the researchers to focus on their production in a commercial scale¹⁵.

Cellulases are involved in the delignification of the pulp without changing the strength of the paper¹⁶. They are effectively used for recycling fibers. Besides, they are also effectively used for separation ink from fiber during deinking process¹⁷

Only few studies have demonstrated application of cellulases in health and medicine. They can be employed for the treatment of phytobezoars disease, which causes concretion of indigestible vegetable and fruit fibers in the gastrointestinal tract that may leads to surgical intrusion. Cellulases have been utilized as excellent ant biofilm agents against pathogenic biofilms. They degrade ‘cellulose’ a major component of biofilms matrix¹⁸.

Cellulases, over many decades, are used in various industrial applications, securing the third rank among enzymes annual sale and expected to exceed the protease in the near future. Cellulase enzymes have got tremendous applications in different industries including biofuel production, paper and pulp industry, detergent industries, animal feeds among others.

Cellulase along with other enzymes is used in the hydrolysis of biomass into sugar and other chemicals. Sugar either hexoses or pentoses are then fermented to bioethanol or other fuel.

With the rapid increase in world population accompanied by increase demand of energy, depletion of fossil fuel, and enhanced greenhouse effect from traditional fuel, there is crucial need to develop or search for cheap, renewable and sustainable sources of energy. Thus cellulases involves in biofuel productions and minimization of energy crisis and environmental pollution¹⁹. However, the bioconversion of pretreated cellulose-based materials at the industrial level into fermentable sugars employ a mixture of enzymes for complete hydrolysis, of which the cost is very high, making bio refining processes economically unfeasible. Thus the search of biocatalysts such as cellulases with novel properties exemplified by high thermostabilty, acidophilicity and high solvent tolerance could help to overcome the cost hurdles. Budihal, 2016 founded that cellulases application in biomass hydrolysis and biofuel productions is currently the subject of numerous studies supported by different agencies across the world²⁰.

Cellulases are used in the paper and pulp industry which has expanded significantly in the last decades from 320 to 395 million tons²¹. Pulping process can be achieved either through mechanical or biomechanical manners. Mechanical pulping such as refining and grinding of the woody raw material results in pulps containing high content of fines, bulk, and stiffness. On the other hand, biomechanical pulping employing enzymes such as cellulases results in around 20–40% energy savings during refining making the process economically feasible and significantly improved hand-sheet strength properties²². Addition of cellulases enhanced the bleachability of softwood kraft pulp and improve the final brightness score comparable to that of xylanase treatment²³.

Cellulase can be used in waste management. For instance, cellulases are used in the conversion of cellulosic municipal solid wastes to desirable chemicals and energy. Cellulases benefits in minimizing the effect of cellulose waste on our environment and driving the conversion of the pollutants to an alternative source of energy and chemicals thus displacing our growing dependence on fossil fuels²⁴.

Cellulase has a great potential to be used in the animal feeds industry²⁵. Cellulase can be used in the pretreatment of agricultural silage and grain feed to enhance nutritional value and performance of animals²⁶. Similarly, addition of cellulase, along with other enzymes, can eliminate anti-nutritional factors present in the feed grains such as arabinoxylans, cellulose, dextrins, inulin, lignin, pectin, β-glucan, and oligosaccharides by degrading them. This in turn enhances the nutritional value and improves animal’s health and performance²⁷. Cellulases are also used in the laundry and detergent industry which is one of the most popular markets for enzymes sale accounting for 20-30%, with lipase and proteases are major enzymatic component. An innovative approach recently adopted in this industry is the use of alkaline cellulases, protease and lipase results in a crucial improvement of color brightness and dirt removal from the cotton blend garments.

The most successful and popular application of cellulases is textile industry. Cellulases are used in textile wet processing such as finishing of cellulose-based textiles, biostoning of jeans and biopolishing of cotton and other cellulosic fabrics in order to improve hand and appearance²⁸.

Cellulase enzymes along with glucanase can be used to improve both quality and yields of the fermented products such as wine and beverages. For examples, during wine production, cellulase, pectinases, glucanases, and hemicellulases are used to improve color extraction, skin maceration, must clarification, filtration, and finally the wine quality and stability. Addition of β-glucosidases can increase the aroma of wines by hydrolyzing glycosylated precursors into their aglycones and glucose²⁹.

Behera, 2016 applied cellulose in agriculture where they are used to hydrolyze the cell wall of plant pathogens thus controlling the plant infection and diseases³⁰. Many cellulolytic fungi including Trichoderma sp., Geocladium sp., Chaetomium sp., and Penicillium sp. are known to play a key role in agriculture by enhancing the seed germination, rapid plant growth and flowering, improved root system and increased crop yields. Cellulases have also been used for the improvement of the soil quality³¹. In addition, Zang et al., 2017 used cellulase in food processing during fruit and vegetable juices manufacturing to improve extraction³². Furthermore, applications of cellulases along with macerating enzymes has been found to increase extraction of olive oil under cold processing conditions and to improve its antioxidants and vitamin E contents ³³. Moreover, humans is known to poorly digest cellulose fiber and taking a digestive enzyme product containing cellulases like Digestin help to relieve digestive problems such as malabsorption. Finally, an interest in applying cellulases enzymes in chemical analysis such as diagnostic and food analysis has been considered³⁴.

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Received on 10.12.2019 Modified on 09.02.2020

Research J. Pharm. and Tech. 2020; 13(11):5635-5641.

DOI: 10.5958/0974-360X.2020.00982.8