Role Of Enzymes In Animal Nutrition: A Review
A peer-reviewed journalPSM Veterinary Research2016 Volume 1 Issue 2 Pages 38-45ISSN: 2518-2714www.psmpublishers.orgReview ArticleOpen AccessRole of Enzymes in Animal Nutrition: A Review1*2222Muhammad Imran , Mubashir Nazar , Muhammad Saif , Muhammad Ahsan Khan , Sanaullah , Muhammad22Vardan , Omer Javed12Institute of Biochemistry and Biotechnology, Department of Animal Nutrition, University of Veterinary and Animal Sciences, Lahore54000, Pakistan.Received: 21.Jul.2016; Accepted: 23.Sep.2016; Published Online: 30.Sep.2016*Corresponding author: Muhammad Imran; Email: mirzaimran42@gmail.comAbstractSupplementation of the specific digestive enzymes in feed improves its nutritional value by increasing its digestion efficiency andenzymes help in the breakdown of anti-nutritional factors which are present in feed ingredients. The key benefits of enzymesimprove feed efficiency and reduce the cost of production of meat and eggs. Enzymes improve the consistency of feed that helps inmaintenance of gut health and digestion process results in overcome the growth of disease causing bacteria. Phytases act onphytate and release phosphorus from phytate, while beta Glucanase acts on non-starch polysaccharides and break down the fiber.Proteases act on protein and improve its digestibility. Cellulases act on cellulose polysaccharides and break down the fiber andAlpha Amylases act on starch and improve its digestibility. All enzymes are used extensively in textile industry, leather industry,waste managements, food industry, syrup making, pulp industry, detergents, paper industry, and in animal feeds to increase itsdigestibility. These digestive enzymes increased growth performance and quality of meat.Keywords: Cellulase, Phytase, Amylase, Protease, Animal nutrition.To cite this article: Imran, M., Nazar, M., Saif, M., Khan, M.A., Sanaullah., Vardan, M., Javed, O., 2016. Role of Enzymes inAnimal Nutrition: A Review. PSM Vet. Res., 01(2): 38-45.in animal feed is phytase, which is used worldwide andaccounts for 50% of all the enzymes used in feed industry.Other enzymes, mainly polysaccharides degradingenzymes (non-starch) accounts the rest (Selle andRavindran, 2007).Anti-nutritional factors are problematic for normal feeddigestion, results in low meat and egg production causeslow feed efficiency and digestive upsets. Feed enzymeswork to make the nutrient (starch, protein, amino acids andminerals, etc.) available from the feed ingredients. Feedenzymes also help to reduce the negative impact of animalproduction over environment by reducing the animal wasteproduction. These Enzymes are proteins that are ultimatelydigested or excreted by the animal, leaving no residues inmeat or eggs (Greiner and Konietzny, 2006).Phosphorus is vital mineral for animals to aid severalfunctions. In past, insufficient utilization of phytate P bypoultry required addition of inorganic Phosphate (P) in dietto meet their nutritional requirements. Due to lessendogenous phytase activity, two thirds of (P) in poultryfeeds of plant origin is secreted without digestion. Thephytase decrease (P) excretion up to 50% which will notonly decrease environmental pollution but also saveinorganic (P). Most of the commercially phytases areINTRODUCTIONDigestive Enzymes are required to digest feed in allanimals and these enzymes are either produced by theanimal body itself or by the beneficial microbes present intheir gastro intestinal tract. Animals are not able to digestabout 15-25% of the feed they eat, because the feedcontain some indigestible components and or the animalbodies lack the specific enzyme which is required for thedigestion of those specific feed nutrients (Konietzny ases that are capable of initiating thestepwise dephosphorylating of phytate (myoinositol); themost ample inositol phosphate in landscape. They havebeen known in plants, microorganisms and animal tissues(Konietzny and Greiner, 2002).Feed cost is the largest cost (60-70%) in livestock andpoultry production systems. To minimize this cost, manyproducers supplement feed with certain enzyme additives,which enable them to produce more meat per animal or toproduce the same amount of meat in cheaper and fasterway (Vohra and Satyanarayana, 2002).Digestive Enzymes are being used in animal feedssince 1980s because of their economic, environmental andhealth related benefits. The most commonly used enzyme382016 Pakistan Science Missionwww.psm.org.pk
M. Imran et al.PSM Veterinary Research 2016; 1(2): 38-45derivative of fungi, bacteria and recombinant technology(Greiner and Konietzny, 2006).Submerged and solid state fermentation used forproduction of exogenous phytase. One of the major issuesto the industry is to improve the utilization of (P) by thebirds and reduce its content in their excreta.Supplementation of phytase to feeds is the best solution toovercome these problems. Extensive research led to theuse of phytase enzymes in poultry diets and helped toproportionately reduce supplementation of inorganic (P) tothe feed. The efficiency of additional phytase in increasingthe bioavailability of (P) and other phytate bound minerals,digestibility of energy and amino acids in poultry (Selle andRavindran, 2008).phytase was reported to improve use of minerals byanimals (Lei and Stahl, 2001). It was hypothesized thatphytase addition results in a better energy use inmonogastric animals. Enzyme preparations with osaccharomyces pombe and Escherichia coli areavailable commercially (Debnath et al., 2005b). In general,their large-scale production is based on the use ofrecombinant strains of filamentous fungi and yeasts.Today, all phytases used for animal feed application belongto the class of histidine acid phytases; β-propeller phytaseshave been supported for several uses. Impeccablephytases for animal feed should fulfill a sequence of qualitycriteria: they should be effective in discharging phytatephosphate in the digestive tract, constant to repelinactivation by temperature from feed treating and storageas well as low-cost to yield (Debnath et al., 2005b). Adeolaand Cowieson directed (2006) that the effect of microbialphytase on phosphorus release depends on nutritivephytate concentration, the source of phytate, species, ageof animals, mineral concentrations in the diet, phytasesources and phytase dosing (Debnath et al., 2005b).Phytase as an Animal Feed AdditiveHydrolytic enzymes have arisen as feed additions inorder to increase the digestion and absorption of poorlyavailable nutrients from the animal feeds. The firstcommercial phytase products were introduced on to themarket in 1991 (Debnath et al., 2005). The possible uses ofphytase in food treating or the production ofpharmaceuticals were reported and phytases have beenlargely used as animal feed additives in diets mostly forswine and poultry and for fish (Debnath et al., 2005). Thesmall intestine of monogastrics has only a very low ability tohydrolyse phytate due to the lack of significant endogenousphytase activity and little microbial population in the upperpart of the digestive tract. This fact also explains whyphytate phosphorus is poorly available to monogastricanimals (Iqbal et al., 1994; Walz and Pallauf, 2002).Phosphorus is absorbed as orthophosphate and use ofphytate phosphorus by monogastrics will largely depend ontheir ability to hydrolyse phytate. The efficiency of additionalmicrobial phytase in improving the utilization of phosphatefrom phytate is very good to enhance animal nutrition(Simons et al., 1990; Adeola et al., 2006; Augspurger et al.,2006; Garcia et al., 2005). Excretion of phosphate can bedecrease by as much as 50%, which is from anenvironmental viewpoint. The dietary supplementation witha microbial phytase has proved to be the most effective toolfor the animal industry to reduce phosphate excretion fromanimal waste, enabling compliance with clearly usefulenvironmental rules. In adding, phytase supplementationdevelops amino acid availability. Phytate proteincollaboration may bring alterations in protein structure thatcan decline enzymatic action, protein solubility anddigestibility (Garcia et al., 2005).A negative effect of phytate on the nutritive value ofprotein was not clearly established in monogastric animals(Sebastian et al., 1998). While some have suggested thatphytate does not affect protein digestibility (Peter andBaker, 2001), others have found improved amino acidavailability with decreasing levels of phytate (Cowieson etal., 2006). This difference may be at least partly due to theuse of different protein sources. In addition, supplementalMode of action of PhytasePhytase catalyzes the stepwise elimination of.phosphate from phytic acid or its salt phytate The exclusionof the phosphate group starts with a fully phosphorylatedphytic acid (IP6), followed by penta- (IP5), tetra- (IP4), tri(IP3), di- and mono-esters of inositol in downward order ofinclination. This means that the phytases first hydrolyze allof the available fully phosphorylated phytic acid to pentaesters of inositol before they hydrolyze the latter to tetraesters of inositol and so on (Simon and Igbasan, 2002). Inan ideal situation, a complete hydrolysis will result in a myoinositol and phosphate (plus amino acids, minerals andother nutrients which are linked to phytic acid). However, inthe in vivo situation, hydrolysis will be incomplete andtherefore normally result in a mixture of inositol-phosphateesters (e.g. IP5, IP4, IP3). The phytate binding to Ca is alsorelated to phytate ester composition, with adisproportionate decrease in the capacity of phytate to bindCa, e.g. IP3 has approximately 11% of the bindingattraction of IP6.Thus the quick elimination of IP6 and IP5in the stomach will considerably decrease the required ofCa in the small intestine (Simon and Igbasan, 2002).Phytate hydrolysis in the digestive tractThe capacity of a phytase to hydrolyse phytate in thedigestive tract is firm by its enzymatic belongings. Withregard to phytate dephosphorylation in the GIT of animals,it is significant to reflect the low pH in the fore stomach(crop) of poultry (pH 4.0–5.0) and in the proventriculus andgizzard of poultry and stomach of pigs and fish (pH 2.0–5.0) (Simon and Igbasan 2002). The small intestine ofanimals presents a neutral pH environment (pH 6.5–7.5).Two key types of phytases have been known, i) acid39
M. Imran et al.PSM Veterinary Research 2016; 1(2): 38-45phytases show greatest phytate dephosphorylation aroundpH 5.0 and ii) alkaline phytases with a pH ideal of aroundpH 8.0. Animal feeding have convinced that the mainfunctional site of additional phytase in pigs and fish is thestomach (Yan et al., 2002; Yi and Kornegay, 1996). Thesite of phytase action in the gastrointestinal tract of poultryhas received little attention. A phytase that should be activein the small intestine requires a sufficiently high stabilityunder the pH conditions in the stomach and intestine aswell as a high resistance to proteolytic activities, mainly ofpepsin in the stomach and the pancreatic proteases in thesmall intestine. To assurance an efficient phytatedephosphorylation in the crop and stomach, stability in anacid environment and conflict to pepsin are properties thatare highly desirable for extra acid phytases (Jongbloed etal., 1992).of digesta, and helps to revitalize natural peristalsis,enhances the digestive process, increasing the overallnutritional value of diet. Beta Glucanase is a very importantenzyme because monogastric animals cannot produce iton its own, Beta Glucanase helps in the breakdown of plantwalls (cellulose), and increases the overall efficiency ofbinding excess cholesterol and toxins in the intestines fortheir removal. Beta glucanase are also particularly useful inindustrial and agriculture processing applications due to itshigh degree of stability. This enzyme is resistant todenaturation by higher than moderate temperature and pHextremes make it particularly durable. It hydrolyze beta Dglucans components, by passing branch points which oftenserve as blocking points to other exo-acting enzymes. BetaGlucanase is used for commercial food processing incoffee; it performs hydrolysis of cellulose during drying ofbeans, Beta Glucanase also used in textile industry as afading agent. Beta-Glucanase has also been found to beparticularly useful in reducing the coating or biofilm ofCandida (fungus) that can grow in the digestive tract(Whitcomb and Lowe, 2007).β-GlucanaseThe soluble non starch polysaccharides (NSP),Pentosans and mixed linked beta-glucans cannot behydrolyzed by endogenous enzymes and result in poorfeed conservation ratio, reduced body weight gain and wetlitter conditions. The primary mechanism of the antinutritional effects of the soluble NSP activity is related totheir viscous properties, which consequently affect theviscosity of the aqueous fraction in the small intestinecontents. The exaggerated intestinal viscosity affects thedigestion and absorption of nutrients in chicks by reducingglucose and sodium transport into the epithelial cells andreducing the release rate of pancreatic enzymes and bileacids. The enzyme widely used in poultry industry isxylanase and beta glucanases. These enzymes cleave thenon-starch polysaccharides in cereal grains such as barleyor hull-less barley (Whitcomb and Lowe, 2007). Severalmechanisms have been proposed to explain the beneficialeffects of these exogenous enzymes in improving energyand nutrient utilization of hull less barley based diets(Whitcomb and Lowe, 2007). Beta glucans are apolysaccharide made of glucose molecules linked togetherinto long chains that monogastric animals cannot readilydigest. In more familiar terms they are cellulose plant fiber,cereal bran fiber, and parts of certain types of fungi, yeast,and bacteria. As a kind of indigestible fiber, they maybecome viscous in the intestinal tract and slow peristalsis(intestinal contractions).These glucans are also present infeed ingredients like barley, wheat and rye whichcommonly used mostly in commercial diets, causingincrease in the viscosity of ingesta thus results in decreasein the availability of nutrients required for the animal growth(Whitcomb and Lowe, 2007).Endogenous proteasesProteases are the enzymes which degrade proteins;these are categorized by their ability to break down thebonds at certain sites of amino acids. The activities fromendogenous proteases are site specific because theiractivity in the incorrect location can lead to destruction ofthe animal’s own tissues. Pancreas is the chief source ofproteases in the body. Major portion of proteases areproduced as inactive pro-enzymes. These rboxypeptidases and proelastase (Kraut, 1977).Exogenous proteasesProteases are actually protein-degrading enzymeswhich are utilized in poultry and livestock nutrition todegrade storage proteins present in plant materials andprotein containing anti-nutrients in them. Seeds,predominantly belonging to legume family such as soy,contain high amount of storage proteins. These areproteins which are mainly generated during production ofseeds and deposited in the seed to give a nitrogen sourcefor the emerging embryo. Storage proteins can attach withstarch (Yu et al., 2007). Proteases can cleave storageproteins hence help in releasing bound energy-rich starchwhich can then be assimilated by the animal. Major proteinbased anti-nutrient factor is trypsin inhibitor. This is presentin untreated plant based protein sources, such assoybeans. They impair digestion process as they inhibittrypsin, secreted by the pancreas and play role in thebreakdown of protein in small intestine. Processed soybeanmeal contains minimal levels of trypsin inhibitor, thusenhances protein digestibility (Kraut, 1977).Importance of Beta-glucanaseBeta Glucanase digests fiber and helps in betterdigestion of heavy cereal grains such as wheat, barley andrye in diet. Because Beta glucanase hydrolyzes theglucans present in these ingredients thus reducing viscosity40
M. Imran et al.PSM Veterinary Research 2016; 1(2): 38-45Efficacy of exogenous ProteasesThe efficacy of mixtures of enzymes together withprotease has been widely reported. Yu et al., (2007)studied effect of including protease in broiler study, whereboth high and a low protein corn–soy diets were used. Theprotease enhanced soy protein digestion in vitro in a classicsystem that imitated the actual digestive tract results fishmeal and maize were similarly influenced (Yu et al., 2007).Many modes of action have been recommended to explainthe positive effects of proteases in poultry diets. Proteasesmay enhance endogenous peptidase formation hencereduces the necessity for amino acids and energy oraugment the degradation of dietary protein. In addition to it,proteases may cleave proteinacious anti-nutrient liketrypsin inhibitors enhancing the effectiveness with whichbird uses amino acids and reduces protein turnover rate(Huo et al., 1993; Marsman et al., 1997).To confirm previous results which recommended thatexogenous protease are a useful entity in animal nutrition, itis suggested that further research work should be done toclarify mechanism of action, ultimate dose, ideal substrate,as well as to discover the relations between supplementaland endogenous enzyme systems (Marsman et al., 1997).other modules of known or unknown function other thanCBM. Three types of cellulases are required for completehydrolysis of cellulose which are; endoglucanses,exoglucanases and beta-glucosidase BG (Bayer et al.,1995).There is an increased trend of using cellulases in manyindustries. Mostly, cellulases are used in food industry, pulpindustry, paper industry, textile industry and also used indetergents as an additive. These are mainly used in animalfeeds to improve feed digestibility Cellulases have a largershare in world enzyme industry at present. But their pricesare relatively high than other enzymes so that it’s used canbe further increased. Its catalytic activity should be furtherincreased to make it economically better and to makeanimal feed more digestible. In dairy, digestibility can besomewhat bearable but in poultry, it should increase starchdigestibility to overcome energy deficiency. Cellulasesperformance should be further increased for the bettercellulose hydrolysis understanding. In that way we can alsounderstand the relationship of molecular structure, andfunction of cellulose (Bayer et al., 1995).Cellulase Enzyme Systems for Cellulose HydrolysisTo utilize cellulase, two strategies are adopted bycellulolytic microorganisms. First one is discrete noncomplexed cellulase and second is complexed cellulase.Mostly cellulose is degraded by secretions of cellulyticmicro-organisms. A set of cellulase has a CBM and acatalytic module. CBM and catalytic modules are attachedwith each other by a linker peptide which is flexible innature. CBM is present at C terminal or N terminal ofmodule and its position doesn’t affect its function in mostcases. Large complexes of multi-enzymes having morethan one million molecular mass are produced byanaerobic micro-organisms mostly that are known ascellulosomes. These cellulosomes are bounded to thesurface of micro-organisms mostly. These cellulosomescan also be produced by some bacteria. Bacteria can alsoproduce free cellulases. CBM in not present in thecellulosome enzymes mostly. CBM is present in a proteincalled scaffoldin (Arnold, 2001; Bayer et al., 1995).Mechanism of Action of Exogenous Amylaseand ProteaseThe composition of the diet can affect the functioning ofdigestive system (Starck, 1999). The true value ofexogenous proteases may reduce maintenance energydemands (also amino acid requirements) rather improvingideally digestible energy only. Proteases are rarely fedseparately rather found commonly as portion of an enzymecocktail, mainly involving glucanases, xylanase
from phytate is very good to enhance animal nutrition (Simons et al., 1990; Adeola et al., 2006; Augspurger et al., 2006; Garcia et al., 2005). Excretion of phosphate can be decrease by as much as .
Restriction enzymes and DNA ligases represent the cutting and joining functions in DNA manipulation. All other enzymes involved in genetic engineering fall under the broad category of enzymes known as DNA modifying enzymes. These enzymes are involved in the degradation, synthesis and alteration of the nucle
20 Production of industrial enzymes and some applications in fermented foods 622 A. Godfrey 20.1 Introduction 622 20.2 Brief history of industrial enzymes 622 20.3 Modem approach to enzyme production 625 20.4 Enzymes from animal materials 626 20.5 Enzymes from plant materials 629 20.6 Principal steps in extraction of animal and plant tissues 630
metabolism? We can group enzymes together according to the types of reactions they catalyse. –Hydrolase enzymes control hydrolysis reactions. –Oxidoreductase enzymes control redox reactions. –Transferase enzymes move whole chemical groups (eg. methyl, amino, carboxyl). –Isomerase enzymes change the shape of a molecule (creating an .
Enzymes in Organic Chemistry! March 25th, 2013! Enzymes Enzymes are biological catalysts. They increase the rate at which equilibrium is reached, but they do not affect the equilibrium. Enzymes differ from ordinary chemical catalyst
4 CHARACTERISTICS of Enzymes – 1. Enzymes do not make anything happen that couldn’t happen on its own, just makes it happen faster. 2. Enzymes are not used up in reactions. They can be used over and over again! 3. Enzymes are highly specific: each enzyme catalyzes a specific chemical rea
Organisms use protein catalysts called enzymes to accelerate many metabolic reactions to useful rates. Enzymes are mainly made of proteins, although many enzymes also incorporate non-protein cofactors, such as vitamins or metals. Enzymes lower the Ea of a reaction because substrates bind to a specific
animal. Say the good qualities of the 2nd place animal over the 1st place animal. List why the 2nd place animal does not win the class. (bad qualities) Say why 2nd place animal beats 3rd place animal by stating only the good qualities of the 2nd place animal. Say the good qualities of the 3rd place animal over the 2nd place animal.
Enzymes are compounds that facilitate chemical reactions. These compounds are mostly proteins found in living organisms and are very important for cells to live and function. For example, the food that you eat is broken down into smaller pieces by different enzymes known as the digestive enzymes. Some
