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Production of Dextrose and Maltose Syrups Using an Enzyme Derived from Rice

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Production of Dextrose and Maltose Syrups Using an Enzyme Derived from Rice Europaisches Patentamt J European Patent Office © Publication number: 0 127 291 Office europeen des brevets A1 (12) EUROPEAN PATENT APPLICATION @ Application number: 84302289.8 © Int. CI.3: C 12 P 19/20 C 12 P 19/22 © Date of filing: 04.04.84 © inventor: © Priority: 20.05.83 US 496386 Line, William F. 5200 S. Tuckaway Blvd. Greenfield Wisconsin 53221 (US) © of of Date publication application: © 05.12.84 Bulletin 84/49 Inventor: Chaudhary, Vinod K. 9496 North Green Bay Road Brown Deer Wisconsin © Designated Contracting States: 53029(US) DE FR GB @ Inventor: Chicoye, Etzer © Applicant: Miller Brewing Company 4374 N. Menomonee River Parkway Milwaukee 3939 W. Highland Boulevard Wisconsin 53225(US) Milwaukee Wisconsin 53223(US) © Inventor: Mizerak, Robert J. N8 3071 0 Cherokee Trail Waukesha Wisconsin 531 86(US) © Representative: Wynne-Jones, John Vaughan et al, Wynne-Jones, Laine & James 22, Rodney Road Cheltenham Gloucestershire GL50 1 JJ(GB) © Production of dextrose and maltose syrups using an enzyme derived from rice. ©A A sugar syrup is prepared by saccharifying a thinned starch hydrolyzate at a pH of about 4.5 to about 7 and a temperature above about 45°C with a heat-stable pullulanase obtained from rice, and an @-1,4a-1,4 carbohydrase.Thecarbohydrase. The pullulan- ase employed is free of maltase and transglucosidase activities. In a preferred embodiment, a dextrose syrup is prepared by saccharifying the thinned starch hydrolyzate with glucoamylase and the rice debranching enzyme at a pH of about 5 and at a temperature of about 55°C. A method of preparing a maltose syrup using the rice debranching enzyme is also disclosed. o CM is CM 0. Ill Croydon Printing Company Ltd The present invention relates generally to the field of making starch-derived dextrose or maltose syrups. More particularly, it relates to a method of preparing dextrose or maltose syrups from starch using a heat- stable debranching enzyme extracted from rice. Prior to the advent of enzymatic saccharification, starch derived syrups were produced by straight acid hydrolysis. The main disadvantage of this process was that acid hydrolysis was non-specific and yielded syrups where the composition was: (1) dependent on the dextrose equivalent (D.E.) of the final syrup, and (2) fixed at any given D.E. These syrups would always contain dex- trose, maltose, higher sugars (maltotriose, maltotetrose, etc.) and dextrins in certain proportions depending on the D.E. of the resultant syrup. Attempts to produce dextrose syrups by straight acid hydrolysis resulted in the production of unacceptable quantities of non- saccharide breakdown products, e.g., furfural. This problem was overcome when the starch industry abandoned non-specific acid saccharifications in favor of specific enzyme catalyzed saccharifications. High dextrose syrups have been important to the starch derived syrup industry (hereafter industry) for some time. These syrups have been used as sweetening adjuncts in the formulation of various foods and bev- erages and more recently as the substrate stream for the production of high fructose corn syrups. The discovery that glucoamylase could be used to saccharify starch to dextrose represented a significant breakthrough in the industry. Using this enzyme, the industry was able to: (1) minimize formation of sugars having a higher degree of polymerization (DP) and other by-products which were inherent with the acid process, and hence (2) produce syrups which contained 92-95% w/w dextrose while operating at a higher dissolved solids level than was possible using acid. The production of high dextrose syrups by glucoamy- lase is not without disadvantages. When a thinned starch hydrolyzate of a low solids content is saccharified with a pure glucoamylase preparation, the dextrose syrup obtained normally has an extremely high dextrose content of 97% or higher. In addition, it is essentially free of non-dextrose saccharide impurities. However, if the starch hydrolyzate solids are increased to the level economically required by the industry, the dextrose content of the resultant syrup substantially decreases and is accompanied by an increase in higher DP saccharide impurities. Nevertheless, industry had accepted a syrup of a lower dextrose content than desired in order to take advantage of the economics which are achieved by conduc- ting the saccharification at the higher starch solids level. In similar fashion, the industry began utilizing maltogenic enzymes, similar to malt diastase, to produce high maltose syrups. Malt diastase is capable of saccharifying starch to produce syrups containing from 50-55% maltose, at dissolved solids levels which are acceptable to the industry. There are three basic classes of starch debranching enzymes. They are the glucoamylases, the isoamylases, and the pullulanases. Basically, pullulanases cleave the a-1,6 linkages of pullulan (an @-1,6 polymer of maltotriose isolated from a mold cell wall) to yield maltotriose. Pullulanases are specific for @-1,6 link- ages and can debranch the a-1,6 linkages of starch to produce a-1,4 polysaccharides which can be converted by a-1,4 carbohydrases to sugars fermentable by brewer's yeast. Due to their effectiveness in hydrolyzing a-1,6 linkages, inclusion of a debranching enzyme in the saccharification increases either the yield (maltose) or rate of produc- tion and yield (glucose) of the desired product. Most commercial fungal glucoamylases do possess debranching activity (i.e., a-1,6 glycosidase activity), but at a much lower level than a-1,4 activity. Therefore, the inclusion of a pullulanase augments the relatively weak a-1,6 activity of glucoamylase, resulting in faster hydrolysis of the a-1,6 linkages, and an increased rate of glucose production from the resulting a-1,4 polysac- charides. In the commercial production of glucose using gluco- amylase it is most common in the industry for economical reasons to use an acid or enzyme thinned starch hydroly- zate having a pH of about 4 to about 5 which is about the optimum for the glucoamylase and a temperature above 50°C. It would be advantageous to have a pullulanase that can operate efficiently under those pH and tempera- ture conditions. We have discovered that a debranching enzyme (pul- lulanase) extracted from rice can be used both in the preparation of high dextrose syrups under the most de- sirable commercial production conditions and in the production of high maltose syrups if the debranching enzyme is free of maltase and transglucosidase activi- ties. It is the primary object of the present invention to disclose a method of preparing high dextrose syrups under commercial pH and temperature conditions which employs both glucoamylase and a pullulanase derived from rice. Further objects of the invention are to disclose enzyme preparations containing a debranching enzyme extracted from ungerminated or germinated rice in which the enzyme is free of contaminating maltase and trans- glucosidase activities, methods of preparing such enzyme preparations, and a method using the enzyme preparation in the production of high maltose syrups. In the practice of the method of the present inven- tion, a sugar syrup is prepared by saccharizing a thinned starch hydrolyzate at a temperature above about 45°C with an enzyme system which includes an a-1,4 carbohydrase and a heat-stable a-1,6 debranching enzyme (pullulanase) derived from rice which is free of both maltase and transglucosidase activities. The debranching enzyme from rice has significant advantages over the pullulanases previously used in that it effectively debranches in a pH range of about 4.0 to about 6.0 and has an optimum pH of about 5. Furthermore, it is surprisingly heat stable at about 45°C to about 60°C. Thus it can be used to prepare dextrose at a pH near the optimum for glucoamylase and under commercial temperature conditions. The invention also relates to a method of obtaining enzyme preparations from rice in which the debranching enzyme is free of maltase and transglucosidase activities and methods of removing the contaminant activities from preparations containing the debranching enzyme. The preferred enzyme preparation containing the debranching enzyme or pullulanase, which is free of maltase and transglucosidase activities, is prepared as described below. When seed or polished rice is the source, a pul- lulanase preparation may be obtained, which is free of the maltase and transglucosidase activities, by ex- tracting the rice in an aqueous buffer having an ionic strength<.02M buffer salts; preferably between 0-.008M. When an extraction medium having an ionic strength much above .02M buffer salts is used, increasing quantities of the maltase and transglucosidase activities are extracted. In the preferred method, the rice is slurried in water at about 50°C for about 3 hours. The enzyme solution may be clarified by centrifugation, and the supernatant further purified by diafiltration and then concentrated to obtain an enzyme preparation containing the debranching enzyme free of the undesirable maltase and transglucosidase activities. When malted rice is the source of the debrancher, the maltase and transglucosidase activities are coex- tracted with the pullulanase even when no buffer salts are added. Therefore, it is another objective of this invention to disclose methods of removing these contami- nants from extracts of either polished or malted rice which contain them. The maltase and transglucosidase activities may be removed from pullulanase containing extracts by adsorbing one activity from another on weak ion exchangers. In one method, pullulanase is adsorbed on a weak anion exchanger, e.g. DEAE cellulose, under conditions which reject the components having maltase and transglucosidase activities. The pullulanase is then eluted from the resin with an ionic strength gradient. In the preferred method, the components having maltase and transglucosidase activities is adsorbed on a weak cation exchange resin, e.g. carboxymethylcellulose or IRC-50 under conditions which reject pullulanase (i.e. buffer salts not exceeding 0.05M and pH about 5 to about 7).
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