CARPATHIAN JOURNAL OF FOOD SCIENCE AND TECHNOLOGY

journal homepage: http://chimie-biologie.ubm.ro/carpathian_journal/index.html

APPLICATION OF STARCH PROCESSING IN FOOD TECHNOLOGY-A REVIEW Saeideh Esmaeili1, Zohreh Noorolahi2*

1Department of Food Technology Research, National Nutrition and Food Technology Research Institute, Faculty of Nutrition Sciences, Food Science and Technology, ShahidBeheshti University of Medical Sciences, Tehran, Iran. 2Department of Food Science and Technology, Faculty of Agriculture, TarbiatModares University, Tehran, Iran. *[email protected]

Article history: ABSTRACT Received: Starch is an important storage compound in plants that has many benefits 18 April 2017 for human beings. It has complex structure and made of two polymers: Accepted: amylose and amylopectin; so the combination of enzymes is needed for its 8 September 2017 decomposi.tion Many of these enzymes exist in natural resources. Keywords: In industry, starch is used in producing different compounds. Some of Starch; them are made by chemical methods but others are produced by just Processing Enzymes; enzymes. Starch processing enzymes are categorized into two groups based (endo, exo); on their operation. The first group are that hydrolyze glycoside De-branched enzymes; bonds by water as endo and exo. The second group are glocanohydrolases Transferses. which break one glycoside α-1.4 bond and creates a new glycoside α-1.4 or α-1.6 linkages. The aim of this article is a general review of these enzymes operation and application in food industry.

1. Introduction sources. There are several methods to extract The starch is an important nutrition starch. Each method has different efficiency of carbohydrate for human being which is stored extraction and the obtained starch has different in leaves, glands, seeds and roots of plants. practical properties too. During extraction, This compound is the second plentiful every damages to the crystalline phase of starch heterogeneous polysaccharide after cellulose and depolymerizing of it is undesirable (Lee et that produced by the plants (Yamada et al., al., 2007). The most common method of starch 2009, Zeeman et al., 2010, Roy Goswamiet al., extraction is grinding the soaked raw 2015). The most known sources of starch are substances for breaking cells' wall, separating cereals, potato, and tapioca which are used for substances by different sieves and finally starch extraction moreover direct consumption separating starch from slurry by decanters or (Whitehurst and van Oort, 2010). Corn, wheat centrifuges (Daiutoet al., 2005; Zhang et al., and potato are mostly used for producing 2009). In another method, fractionation is used industrial starch in Europe and America, for separating starch from protein. In this whereas in Asia, casava, rice, sweat potato, method, grinding is done for dry substances yam and arrow root are used too. The annual and then air is used for separating starch. This production of starch is around 48 ×106 ton in method is efficient and easy and there is no the world which nearly 70% of this is used in need to moving plenty amount of starch food industry (Daiuto et al., 2005). solution (Lee et al., 2007) but the produced Starch is stored in granolas. The shape and starch shows weaker practical properties size of the granolas are varying in different comparing with the starch from moist method 114

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(Tian et al., 1999). In some methods, alkali is of fewer long branches (Srichuwong et al., used for solubilizationof protein and extraction 2005; Yoo and Jan., 2002). The structure of of starch (Cardosoa et al., 2007). The produced starch components is shown in Figure 1. The starch from this method has got high purity construct, molecular weight and proportion of (Puchongkavarinet al., 2005) but comparing amylose to amylopectin is different in extracted with the one produced from moist method, it starch from different plant sources. This leads shows lower pasting temperature and higher to diverse characteristics invarious types of pasting viscosity (Dokicet al., 2010; Lai et al., starch (Syaharizaet al., 2010; Srichuwong et al., 2004; Han and Hamaker, 2002). 2005). The waxy starches consist of plenty amount of amylopectin but the hylon consists 2. Types of starch processing enzymes of more than 50% of amylose (van der Maarel The natural starch is made of about 20% and Leemhuis. 2013). At the moment, near amylose and 80% amylopectin. Amylose is 30% of worldwide production has linear polymer of glucose with α-1.4 bounds allocated to starch processing enzymes.In and its molecular weight is around 106 Dalton Table 1 most commercial applications of starch whereas amylopectin has 5% α-1.6 links in processing enzymes in food industry has been addition to mentioned bonds and its weigh is .shown about 108 Dalton. In this way amylopectin has a lot of small branches but amylose is composed

Amylose: linear polymer of glucose with α -1,4 links

Amylopectin; glucose polymer with α -1,4 links and branched with α -1,6 links

Figure 1.Chemical structure of amylose and amylopectin (Tucker and Woods, 1995)

Table 1. The most common commercial application of starch processing enzymes in food industry Application Enzyme/Enzymes Starch liquefaction α- Starch saccharification α-amylase, glucoamylas,,isoamylase, maltogenic amylase Baking industry α-amylase,

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Anti-staling α-amylase, β-amylase, pullulanase, debranched enzymes, branching enzymes, maltogenic amylase, glucoamylase, cyclodextrin glucanotransferases Cycloamylose production α-glucanotransferases

As starch polymer has complex Generally, the effective enzymes on starch constructer, combination of enzymes is needed can be categorized into four groups: endo- for decomposing it to smaller parts or amylases, exo-amylases, de-branched enzymes transferring oligoglycosidic bonds or creating and transferses (Hii et al., 2012). The best- new bonds (Bertoldo and Antranikian, 2002). known enzymes affecting on starch belong to The important enzymes which are usually used glycoside hydrolases families 13, 15 and 28 for biotechnology field and also starch process (Whitehurst and van Oort, 2010). are called amylase. In one category, starch Specificationsof starch processing enzymes enzymes are classified in to two groups: a) have been shownin Table 2. Table hydrolases which hydrolyze glycosidic bonds 3alsoincludes enzymessubstrates and products by water in two ways endo and exo; b) derived from the effects of these. glocanotransferases which break one α-1.4 bound and create new α-1.4 or α-1.6 bound.

Table 2. Characteristics of starch processing enzymes Activity Enzyme name EC Enzyme Group of α-1,4 linkages α-amylase 3.2.1.1 Endoamylases Hydrolysis of α-1,4 and α-1,6 Glucoamylase 3.2.1.3 Exoamylases linkages Hydrolysis of α-1,4 linkages α-Glucosidase 3.2.1.20 Hydrolysis of α-1,4 linkages β-amylase 3.2.1.2 Hydrolysis of α-1,6 linkages Amylo-1-6-glucosidase 3.2.1.33 De-branched enzymes Hydrolysis of α-1,6 linkages Pullulanase type I 3.2.1.41 Hydrolysis of α-1,4 and α-1,6 Pullulanase type II 3.2.1.41 linkages Hydrolysis of α-1,4 linkages Pullulan types I 3.2.1.135 () Hydrolysis of α-1,4 linkages Pullulan hydrolase types II 3.2.1.57 (isopullulanase) Hydrolysis of α-1,6 linkages Isoamylase 3.2.1.68 Hydrolysis of α-1,4 linkages Cyclodextrin 2.4.1.19 α- and formation of new α -1,4 glucanotransferases glucanotransf linkages erases Hydrolysis of α-1,4 linkages 4-α-glucanotransferase 2.4.1.25 and formation of new α -1,4 linkages Hydrolysis of α-1,4 linkages Branching enzyme (Q- 2.4.1.18 and formation of new α -1,6 enzyme)

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linkages

Table 3. Substrates and products obtained from acting ofstarch processing enzymes Product/products Mainsubstrate Enzyme name Linear and branched Starch α-amylase oligosaccharides, α-limit dextrins High glucose syrup Starch Glucoamylase 1- Glucose, isomaltose, 1-Starch α-Glucosidase isomaltortiose 2-Oligosaccharidescontainingmaltose 2-Isomalto-oligosaccharides 3-Branched Oligosaccharides likely (IMO) panose and isopanose β-limit dextrins Starch β-amylase Side chain containing of one glucose amylo-1-6-glucosidase (product of transglycosylase enzyme) Maltotriose Pullulan, Amylopectin Pullulanase type I Maltose, maltotriose Pullulan, Amylopectin Pullulanase type II Maltose, maltotriose Amylopectin, glycogen Isoamylase ϒ-cyclodextrins, gluco- Compounds containing of Cyclodextrin و α، β oligosaccharides with cycle α- someconsecutive α-1,4 glycosidic bond glucanotransferases 1,4 bonds (scchardinger sugars) Glycogen, amylopectin Compounds containing of 4-α-glucanotransferase someconsecutive α-1,4 glycosidic bond

Amylopectins and glycogen with Starch, glycogen Branching enzyme (Q- more side chains enzyme) maltose syrups (Souza and Magalhaes, 2010; 2.1. Endo-amylases Tucker and Woods, 1995). These enzymes can break α-1.4 glucosidic bonds that exist in inner part of amylase or 2.2.Exo-amylases amylopectin chain. Among these enzymes, These enzymes which consist of there is α-amylase (EC1.1.2.3) which breaks glucoamylase (EC 3.2.1.3) and α glucosidase mentioned bonds randomly but when reaches to (EC 3.2.1.2) break α-1.4 and α-1.6 bonds α-1.6 linkages, these operation is stopped. In between glycosides from non-reducing end of this way, they produce linear and branched amylase and amylopectin and therefore, they oligosaccharides and α-limit dextrins produce glucose. β-amylases (EC 3.2.1.2), (Kammoun et al., 2008; Van der Maarel et al., which also belong to this group, break α-1.6 2002). These enzymes are industrially obtained bonds exclusively from the end of non- from bacterial and fungal sources. The bacterial reducing and therefore produce maltose and β- types of α-amylases are really resistant to high limit dextrins (Haki and Rakshit, 2003; temperature, react in normal pH and need to Bertoldo and Antranikian, 2002). calcium ion for their activity. While the fungal α-amylases are nearly sensitive to temperature. 2.2.1. β-amylases These enzymes are maltogenic and their main These enzymes are exo-acting. They product are maltose and other oligomers; so cannot separate α-1.6 branches like α-amylases, they are not used for liquefaction but are used and can't turn the obstacles; so they produce as substitute of β-amylase for producing high high molecular weight dextrin that is well- known as β-limit (Li and Yu, 2011). These enzymes accompany with de-branched 117

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enzymes are used for producing syrups in These enzymes catalyze hydrolysis of α- industry. The maltose syrups are hygroscopic 1.6 bonds and tend to separate amylopectin and have more constant color than glucose branches.This tendency is the main difference syrups. Moreover, they are used in between de-branched enzymes and other confectionary industry and producing frozen hydrolysis enzymes because the main place of desserts because of less crystallization and other hydrolysis enzymes is α-1.4 bonds (Hiiet adhesion (Tucker and Woods, 1995). al., 2012). These enzymes are categorized into two main groups: direct de-branched and 2.2.2. Glucoamylase indirect de-branched enzymes (Fogarty and These enzymes which are known as Kelly, 1990). amylo-glucosidase or sugar-making amylase separate α-1.4 bonds and in lower extent α-1.6 2.3.1. Indirect de-branched enzymes bonds from non-reducing end, similar Amylo-1,6-glucosidase (EC 3.2.1.33) is an pullulanase type II. (Whitehurst and van Oort, indirect de-branched enzyme. In the beginning , 2010). The high activity of this enzymewould the substrate of this enzyme has to be reformed produce high glucose syrups. This activity is by another enzyme because this enzyme can done by using a lot of enzymes but this amount hydrolyze just the side chain which consists of of enzyme may cause undesirable side one glucose molecule. For this reason, at first reactions such as return reaction and producing oligosaccharide was taken with isomaltose and maltose and therefore may transglucosylase enzyme (4-α- decrease final output. These enzymes are acid glucanotransferase, EC 2.4.1.25) and substrate like and sensitive to temperature. In industry, was ready for acting of this enzyme they are used for hydrolysis dextrins to glucose (Nakamura, 1996). This enzyme does not syrup in saccharification (Hii et al., 2012; widelyused in industry (Hii et al., 2012). Tucker and Woods, 1995). 2.3.2. Direct de-branched enzymes 2.2.3. α-Glucosidase These enzymes directly hydrolyze α-1.6 α- are also exo-acting bonds in unreformed substrates. Among these enzymes that separate amylose, amylopectin enzymes are and isoamylases. and oligosaccharides with maltose from non- reducing end and produce glucose (Latorre- 2.3.2.1. Pullulanases Garcia et al., 2005; Tatsumi and Katano, 2005). Other names ofpullulanases EC 3.2.1.41 When the maltose concentration is high are α-dextrine 6-glucanohydrolase, enough, transglycosylation reaction is done by amylopectine 6-glucanohydrolase, pullulan 6- this enzyme and therefore maltose changes to glucanohydrolase and limit dextrinase. These isomaltose (two glucose with 1, 6 linkage). In enzymes are extracted from microbial sources the next stage isomaltose will be glycosylated and arehydrolyzed α-1.6 bonds in pullulan (the and will produce isomaltotriose. Branched repeated units contain of three glucose residues oligosaccharides like panose and isopanose can with α-1.4 bonds which are linked together by also be glycosylated by this enzyme. These one α-1.6 bond) (Zareian et al., 2010; compounds are generally well- known as Kuroiwaet al., 2005; Roy and Gupta, 2004). isomalto-oligosaccharides (IMO) which are The final product by these enzymes is produced as prebiotic fibers in China and Japan maltotriose (Kunamneni and Singh, 2006). (Whitehurst and van Oort, 2010). Pullulanases type I hydrolyze α-1.6 bonds and produce branched dextrins. These enzymes are 2.3. De-branched enzymes like isoamylases. Pullulanases type II hydrolyze both α-1.4 and α-1.6 bonds andoften 118

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generate maltose and maltotriose. Recent hydrolyzes α-1.6 bonds in pullulan and enzymes are similar toglucoamylase and are amylopectin whereas isoamylase hydrolyzes commercially used in saccharification these linkages in amylopectin and glycogen (Whitehurst and van Oort, 2010). (Mikami et al., 2006). In other words, ,So far five groups of pullulan hydrolyzing pullulanase needs two chains for actions enzymes are reported that are categorized based containing at least two glucose residues with α- on characteristics of the substrate and reaction 1.4 bonds which are joined with α-1.6 bonds of products: whereas isoamylase prefers high molecule Pullulanases type I: they hydrolyze α-1.6 weight substrates. Another difference is their bonds in pullulan and branched source so that the de-branched enzymes in polysaccharides. Pullulanases type II yeasts and molds are mostly isoamylase but (amylopullulanase): they hydrolyze α-1.4 or α- bacterial de-branched are mostly pullulanases 1.6 linkages and are used vastly in starch (Hii et al., 2012; Van der Maarel et al., 2002). processing industry. Both enzymes don't affect Application of only α-amylase or β- on cyclodextrins (Roy et al., 2003; Ben amylase during starch saccharification Messaoudet al., 2002; Duffner et al., 2000). processes produces plenty of α-limit and β-limit Neopullulanases (pullulan hydrolase type I) and dextrins respectively and reduces the final isopullulanases (pullulan hydrolase type II) can viscosity of glucose. For this reason, the use of break α-1.4 bonds and affect on cyclodextrins de-branched enzymes increases efficiency of but not starch. The enzymes which analyze glucose production. The hydrolysis of cyclodextrins faster than starch are called amylopectin and limit dexterins like produced cyclodextrinase (Kaharet al., 2013). Since these dexterins by Klebsiella planticola and Bacillus enzymes are able to recognize the structural acidopullyticus can be done by using bacterial differences between α-1.4 bonds and α-1.6 pullulanase, but using fungal isoamylase is bonds exactly, they are used vastly for limited because of the lower temperature analyzing polysaccharide and oligosaccharide stability and lower pH adaptation with β- structures (Roy et al., 2003). Pullulan hydrolase amylase. type III which were known by Niehause et al, Another problem for using isoamylase in unlike other pullulan hydrolyzing enzymes, can saccharification is its inability in hydrolysis of hydrolyze α-1.4 and α-1.6 bonds in pullulan side chains consisted of 2 and 3 glucose unit in that produce a mixture of maltotriose, panose, α-limit and β-limit dextrins. Therefore the maltose, and glucose (Niehause et al., 1999). simultaneous action of β-amylase and These enzymes can also analyze starch, isoamylase cannot change amylopectin to amylose and amylopectin and produce maltose maltose. On the other hand, β-amylase is and maltotriose (Hii et al., 2012). considered as isoamylse inhibitor. The existence of maltotrios and maltotetraose also 2.3.2.2. Isoamylase inhibits isoamylse action competitively (Hii et Isoamylases (EC 3.2.1.68) can hydrolyze al., 2012). α-1.6 bonds. These enzymes are the only The biggest advantage of using pullulanase known ones which can debranche glycogen instead of isoamylase in saccharification is that completely. They are made of two subunits adding stages of isoamylse is very critical. For with 45000 molecule weight (Zobel, 1992). example adding this enzyme to the hydrolysis system before amyloglucosidase can cause 2.3.2.3. Comparing pullulanase and depolymerisation of amylopectin and therefore isoamylase acceleration of the retrogradation (Guzman- The main difference between these enzymes Maldonado and Paredes-Lopez, 1995). is in their substrates so that pullulanase 119

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2.3.3. Application of de-branched enzymes Substrates of α glucanotrnsferases are the During saccharification process, α-1.6 compounds consist of some consecutiveα-1.4 bonds in starch act as an inhibitor for action of glycosidic linkages like amylose, amylopectin, starch hydrolyzing enzymes and for this reason, maltodextrins and glycogen. α- hydrolysis continues with the usage of de- glucanotransferases belong to glycoside branched enzymes and efficiency of glucose hydrolases (GH) family. Members of this production increases. family break glycosidic bonds and move them Application of glucoamylase alone can to acceptor (usually water). These enzymes can produce plenty of isomaltose. Since this also link separate parts to other sugar and make compound is resistant to hydrolysi,s the new glycosidic bonds (so-called efficiency of final production decreases (Crabb disproportionation reaction) (Oh et al., 2008). and Shetty, 1999; Uhlig, 1998). Using α-glucanotransferase used in industry belong to glucoamylase and pullulanase simultaneously GH 13,57,77 families. All these enzymes are as can prevent by-product isomaltose. In this α-retaining; it means that anomeric situation, pullulanase hydrolyses branch points configuration of new made glycoside bonds is specifically and then glucoamylase hydrolyses similar to broken bonds in substrate (Vocadlo α-1.4 bonds in line chain (Hii et al., 2012). and Davies, 2008). Reaction of these enzymes With utilization of de-branched enzymes at first is started by breaking one α-1.4 together with glucoamylase, the speed of glycosidic linkage in substrate and an enzyme- saccharification increases, the amount of glycosyl intermediate is produced. In the next needed glucoamylase decreases and less stage and after existing the fragmented sugar activity of glucoamulase is needed. In this way, part from acceptor, non-reducing end from the cost of pullulanase usage will be another glucan can enter acceptor site and the compensated by saving in vaporization cost and new bond is made. On the base that whether glucoamylase cost. Application of these two non-reducing end attack from 4-hydroxyle or 6- enzymes in fructose syrup process decreases hydroxyle, the new bonds are as α-1.4- and α- the isomerization expenses too because of 1.6 respectively (Stamet al., 2006; Zona et al., increasing capacity of factory as the result of 2004). decreasing saccharification time (Poliakoff and and Licence, 2007). 2.4.1. The types of α-glucanotransferases Nowadays de-branched enzymes are used Tree types of α-glucanotransferases have in saccharification of starch, production of high been known so far: I. Cyclodextrin α- maltose corn syrup, production of detergents glucanotransferase (CGTAs; EC 2.4.1.19), II. and with CGTAs in production of cyclodextrins 4-α-glucanotransferase (4αGT; EC 2.4.1.25) (Hii et al., 2012). which is sometimes shown as amylo-, disproportionating or D-enzyme too, III. Branching enzyme (BE; EC 2.4.1.18) which is known as Q-enzyme (Van der Maarel and 2-4. α-glucanotransferases Leemhuis, 2013; Leemhuis et al., 2010; Kaper Application of a glucanotrnsferases or et al., 2004). In Table 4 there is industrial AGTAs (EC 2.4.2.XX) is made prevalent in application of these enzymes briefly. two recent decades. These enzymes do not hydrolyze starch as amylases but at first break 2.4.1.1. Cyclodextrin glucanotransferases some parts of amylose and amylopectin (CGTAs) molecules and then makes new bonds again For this group of enzymes the dominant (Van der Maarel and Leemhuis, 2013). reaction is intra-molecular transglycosylation which causes cycle product with 6, 7, 0r 8 120

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glucose residues with α-1.4 bonds that are CGTAs are also used for preventing of called α-, β- and γ-cyclodextrins (Vollu et al., bread staling. Since the structure of this 2008; Qi and Zimmermann, 2005). When the enzyme is highly similar to the structure of amount of glucan acceptor containing one free anti-stalingenzyme, Novomyl, the structural 4-hydroxile group ishigh , CGTAs can shift the change in later enzyme changes it to a CGTAs. glucan intermediate to another glucan chain There are some reports which show that the and do inter molecular transglycosylation. In mutant CGATs types improve the quality of this way, a circular product is created bakery production too (Shim et al., 2007; Kelly (Whitehurst and van Oort, 2013; Van der et al., 2009). Maarel and Leemhuis, 2013). 2.4.1.2. Amylo-maltases or 4αGT 2.4.1.1.1. Application of cyclodextrin This enzyme in contrast to CGTAs does glucanotransferases (CGTAs) intermolecular transglycosylation. In this way, These enzymes exist in bacteria and they break α-1.4 bonds and create new bonds. archaeas which areactive in high temperature. These new bonds are in the form of α-1.4 too. They are considered asthe first industrial If the concentration of glucan acceptor AGTAs (Biweret al., 2002; Leemhuis et al., containing a free 4-hydroxile group is little, 2010). The main usage of these enzymes is these enzymes do intermolecular production of industrial cyclodextrins. α-, β-, transglycosylation and create cyclic molecules and γ-cyclodextrins are considered asgluco containing 15 glucose residues with -1,4α oligosaccharides with cyclic α-1.4 bonds which bonds which are known as Large-ring are known as sacchardinger. These compounds cyclodextrins LR-CD (Srisimarat et al., 2011; have hydrophobic inner part and hydrophilic Kaperet al., 2004; Terada et al., 1999). outer part because the sequence of their glucose residues. Therefore, they can complex with 2.4.1.2.1. Application of Amylo-maltase or hydrophobic compounds and change their 4αGT physical and chemical properties. These In nature, these enzymes participate in compounds are used as antiseptic factor glycogen metabolism in bacteria and also (Whitehurst and van Oort, 2010). In food foundation of amylopectin in plants (Kaper et industry, α-, β-, and γ-cyclodextrins are also al., 2004). But in industry, the amylo-maltases used vastly for taking cholesterol, stabilizing of thermal resistant bacteria are used to transfer aromatic and sensitive compounds, solubilizing a part of amylose to non-reducing end of hydrophobic compounds in water, and amylopectin. The obtained substance is eliminating undesirable taste and odor (Astray composed of the amylopectins with long chains et al., 2009; Szente and Szejtli, 2004; which can produce a white opaque gel with Reineccius et al., 2003). ability of thermal returning. Therefore, this Wacker Chemie Company has offered α- substance is a suitable vegetal gel and can be cyclodextrins as indigestible diet fiber. This used instead of gelatin which is an animal product is obtained from the effect of compound (Euverink and Binnema, 1998). The cyclodextrin glucanotransferases enzyme on starch which is used in this purpose has to the liquefied starch.Mentioned enzyme is contain amylose (Hansen et al., 2009; Hansen extracted from K.oxytoca. This product has et al., 2008). In this process, α-1.4 linkage been produced with KAWAMAX W6 trade between two glucose is broken and a new α-1.4 name and is used as a diet fiber in carbonated linkage is formed (Oh et al., 2008). The new and noncarbonated soft drinks, dairy products, substance is similar to primary substance in and bakery products (Whitehurst and van Oort, reducing power, percebranches, and average of 2010). molecular weight (van der Maarel et al., 2005). 121

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Etenia is a trade name for a thermal reversible insulin and glycemic index less (Van der gel which is produced by AVEBE, a Dutch Maarel and Leemhuis, 2013). company. This substance is obtained by the effect of extracted amylo-maltase enzyme from 2.4.1.3. Q- Enzymes (branched enzymes) Thermus thermophiles bacteria on potato This group of enzymes is completely starch. It is free of amylose and unlike starch, different as they break α-1.4 bonds and link produces thermal reversible gel starch because produced α-glucan to 6-hydroxile groupin a it has amylopectin with side chains containing linear glucan chain which has α-1.4 bonds more than 35 glucose. The only difference itself. Therefore, one branch is made (van der between this gel and starch is its opal. This Maarel and Leemhuis, 2013; Whitehurst and compound is used for making creamy texture in van Oort, 2010). These enzymes are in GH 13 low fat products. Altinget al. applied this and GH 57 families. GH 13 family affects on enzyme for increasing ceramin in yogurt. The amylopectin and amylose whereas the members mentioned enzyme is produced from of GH 57 family affect on just amylose B.amyloquefaciens bacteria by DSM Company (Palomoet al., 2009; Palomoet al., 2011). (Altinget al., 2009; Munet al., 2009). In contrast to most enzymes which are used for 2.4.1.3.1. Application of Q- Enzymes starch processing, this enzyme doesn’t secreted (Branched enzymes) out of cells so the downstream process of its Innature these enzymes are involved in extraction is difficult (Whitehurst and van Oort, constructingof side branches in amylopectin 2010). All modified starch with this enzyme and glycogen (Zeeman et al., 2010; Murakami contain amylopectins with long chains (Hansen et al., 2006). Glycogen branched enzymes et al., 2008). differs from starch branched ones in number of When the high amount of amylose with synthesized α-1.6bonds so that all types of high molecule weight is incubated with high starch branched enzymes make about 3.5 to 5% amount of amylo-maltase, some compounds of α-1.6 bonds whereas the construction of called cycloamyloses are produced. these bonds in glycogen is more than 10 % Cycloamyloses are large cycle compounds (Whitehurst and van Oort, 2010). containing at least 16 glucose residues. Because The ability of these enzymes in breaking α- of the large size of these compounds, they 1.4 bonds and creating α-1.6 instead is lead to make two or more unparalleled spiral. In this products which lack long α-1.4 chains. way a hydrophobic channel is made. This Therefore, they produce dextrins contain short channel is used for conservation of different side chains and as a result do not retrograde and compounds like drugs and also protection of have low viscosity (Spendler and Jorgensen, proteins from deforming (Tomonoet al., 2002; 1997). Novozym company has extracted a Machida et al., 2000). glycogen branched enzyme from The starch that is resistant to digestion Rhodothermus obamensi sthermophile bacteria have been produced by using of amylo-maltase that produces branched dextrin. Since this accompany with a de-branched enzyme like enzyme is stable up to 80°C, it seemed to be pullulanas. These products are called Promitor suitable for starch process (Shinohara et al., RS60 and RS75 and are linearmalto- 2001). So far no branched dextrin has been oligosaccharids with different polymerization produced as anti-stalling factor because of non- degrees which are made in crystal form. commercial production of enzymes (Van der Pancreatic and saliva α-amylases has no effect Maarel and Leemhuis, 2013). The constant on these crystals so usage of these compounds viscosity derivatives of starch are used for comparing with normal starch increases blood paper and texture industry (Bisgaard-Frantzen et al., 1999). Kim et al. in 2008 extracted a 122

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glycogen branched enzyme from Streptococcus compounds, all starch processing enzymes have mutans that delayed retrogradation by changing not been known thoroughly. Therefore many the starch to more branched structure. studying in the field of recognition and Q- Enzymes arealso used for producing application of these enzymes for new products branched dextrins which are digested slowly. is being continued so that production of new The higherthe amount of branch in starch, the refined and practical starch will be seen in harder pancreatic amylose can degrade starch, future. therefore the level of blood glucose remains low (Whitehurst and van Oort, 2010). 4. References Deinococcus radiodorans is able to produce Alting, A.C., van de Velde, F., Kanning, M.W., branched enzyme which changes amylopectin Burgering, M., Mulleners, L., Sein, A. to a branched maltodextrin. This enzyme (2009). Improved creaminess of low-fat accompany with pancreatic amylase releases yoghurt: The impact of amylomaltase- glucose slowly in vitro condition (Palomo et treated starch domains. Food al., 2009). Roquete company has also produced Hydrocolloids, 23, 980–987. a starch with low digestibility by a branched Astray, G., Gonzalez-Barreiro, C., Mejuto, J.C., enzyme accompany with β-amylase (EC Rial-Otero, R., Simal-Gandara, J. (2009). 3.2.1.2) (Dermaux et al., 2007). Using A review on the use of cyclodextrins in maltogenic amylase instead of β-amylose foods. Food Hydrocolloids, 23, 1631– showed similar effect (Le et al., 2009). 1640. Other products yielded by branched Ben Messaoud, E., Ben Ammar, Y., Mellouli, enzymes are cluster cyclodextrins (CCD). L., Bejar, S. (2002). Thermostable These compounds are used in sport drinks. This pullulanase type I from new isolated substance increases the time of being empty in Bacillus Thermoleovorans US105: cloning, stomach and can affect positively on body sequencing and expression of the gene in perseverance. Ezaki Glico Company extracted E. coli. Enzyme and Microbial Technology, a branched enzyme from Aquifexaeolicus 31, 827–832. thermophile bacteria and applied it for Bertoldo, C., Antranikian, G. (2002). Starch- converting corn starch to a cluster hydrolyzing enzymes from thermophilic cyclodextrins. At present, this enzyme is archaea and bacteria. Current Opinion in produced by Nagase Company (Whitehurst and Chemical Biology, 6, 151–160. van Oort, 2010). Bisgaard-Frantzen, H., Svendsen, A., Norman, B., Pedersen, S., Kjaerulff, S., 3. Conclusions Outtrup, H., Borchert, T.V. (1999). In this research the starch processing Development of Industrially Important α- enzymes that are used for modification and Amylases. Journal of Applied conversion of starch and production of various Glycoscience, 46, 199-206. compounds were studied. Some of these Biwer, A., Antranikian, G., Heinzle, E. (2002). enzymes as alpha amylase and glocoamylase Enzymatic production of cyclodextrins. are used in large scale but the others are applied Applied Microbiology and Biotechnology, in smaller scale. Producing ofsweeteners is the 59, 609–617. most common application of these enzymes. Cardosoa, M.B., Putaux, J.L., Samios, D., Some other produced compounds by these Silveira, N.P. (2007). Influence of alkali enzymes have functional properties and their concentration on the deproteinization usage will have high potential influence on and/or gelatinization of rice starch. users' health. Despite performance ofvide Carbohydrate Polymers, 70, 160–165. researches and production ofvarious 123

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