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Glucose Isomerase To Fructose

Carbohydrates - Corn Syrup

Carbohydrates - Corn Syrup

The development of the various types of corn syrups, maltodextrins, and high-fructose corn syrup from corn starch sources could be called one of the greatest achievements in the sugar industry. Corn starch can be hydrolyzed into glucose relatively easily, but it was not until the 1970s that it became a commercially major product bringing about changes in the food industry. The starch is processed and refined from the kernels of corn by using a series of steeping (swelling the kernel), separation, and grinding processes to separate the starch from the other parts of the kernel which is used for animal feed. The starch is hydrolyzed using acid, acid-enzyme, or enzyme-enzyme catalyzed processes. The first enzyme is generally a thermally stable alpha amylase which produces about 10-20 % glucose. Further treatment with the enzyme glucoamylase yields 93-96% glucose. The final Corn Syrup (glucose syrup) products include: dried corn syrup, maltodextrin, and dextrose (glucose). With the development of glucoamylase in the 1940s and 1950s it became a straightforward matter to produce high percent glucose syrups. However, these have shortcomings as used in the sweetener industry. D-glucose has only about 70% of the sweetness of sucrose, on a weight basis, and is comparatively insoluble. Fructose is 30% sweeter than sucrose, on a weight basis, and twice as soluble as glucose at low temperatures so a 50% conversion of glucose to fructose overcomes both problems giving a stable syrup that is as sweet as a sucrose solution of the same concentration. One of the triumphs of enzyme technology so far has been the development of 'glucose isomerase', which in turn led to the commercialization of high fructose corn syrups. Now it is known that several types of bacteria, can produce such gluc Continue reading >>

Us3625828a - Process For Production Of Glucose Isomerase - Google Patents

Us3625828a - Process For Production Of Glucose Isomerase - Google Patents

US3625828A - Process for production of glucose isomerase - Google Patents Process for production of glucose isomerase US3625828A US3625828DA US3625828A US 3625828 A US3625828 A US 3625828A US 3625828D A US3625828D A US 3625828DA US 3625828 A US3625828 A US 3625828A Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.) Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.) C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes C12N9/92Glucose isomerase (5.3.1.5; 5.3.1.9; 5.3.1.18) YGENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS Y10TECHNICAL SUBJECTS COVERED BY FORMER USPC Y10STECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS Y10S435/00Chemistry: molecular biology and microbiology Y10S435/822Microorganisms using bacteria or actinomycetales A novel glucose isomerase enzyme us

Cfr - Code Of Federal Regulations Title 21

Cfr - Code Of Federal Regulations Title 21

CFR - Code of Federal Regulations Title 21 The information on this page is current as of April 1 2017. SUBCHAPTER B--FOOD FOR HUMAN CONSUMPTION (CONTINUED) Subpart B--Listing of Specific Substances Affirmed as GRAS Sec. 184.1372 Insoluble glucose isomerase enzyme preparations. (a) Insoluble glucose isomerase enzyme preparations are used in the production of high fructose corn syrup described in 184.1866. They are derived from recognized species of precisely classified nonpathogenic and nontoxicogenic microorganisms, including Streptomyces rubiginosus, Actinoplanes missouriensis, Streptomyces olivaceus, Streptomyces olivochromogenes, and Bacillus coagulans, that have been grown in a pure culture fermentation that produces no antibiotics. They are fixed (rendered insoluble) for batch production with GRAS ingredients or may be fixed for further immobilization with either GRAS ingredients or materials approved under 173.357 of this chapter. (b) The ingredient meets the general and additional requirements for enzyme preparations in the Food Chemicals Codex, 3d Ed. (1981), p. 107, which is incorporated by reference. Copies are available from the National Academy Press, 2101 Constitution Ave. NW., Washington, DC 20418, or available for inspection at the National Archives and Records Administration (NARA). For information on the availability of this material at NARA, call 202-741-6030, or go to: (c) In accordance with 184.1(b)(1), the ingredient is used in food with no limitation other than current good manufacturing practice. The affirmation of this ingredient as generally recognized as safe (GRAS) as a direct human food ingredient is based upon the following current good manufacturing practice conditions of use: (1) The ingredient is used as an enzyme, as defined in 170.3(o) Continue reading >>

Make Your Own Small-batch, Artisanal High Fructose Corn Syrup

Make Your Own Small-batch, Artisanal High Fructose Corn Syrup

Make Your Own Small-Batch, Artisanal High Fructose Corn Syrup By Dan Nosowitz posted Jun 3rd, 2013 at 3:30pm Think of corn on a hot summer's day. Sweet, delicious, all-American corn. It's stuck in your teeth and you barely care, as your practiced jaw scrapes the pure taste of the season from the cob. Now think of high-fructose corn syrup. You probably don't have an idyllic childhood memory to go along with the sugarglop that's killing both the American people and the American tradition of agriculture . Just a guess! HFCS, as it's called, is a relentlessly common sweetener in everything from soda to bread. It's used because, in bulk, it's incredibly cheap, thanks to agricultural subsidies from the US government that encourage farmers to grow the high-yield, flavorless-when-unprocessed variety of corn used for HFCS. One of the many odd things about high-fructose corn syrup is that you can't really buy the pure stuff in a store. What's even in the stuff? That's what artist and designer Maya Weinstein wondered--except she actually secured the ingredients for her thesis project at Parsons. The DIY HFCS Kit includes all of the delicious materials that go into our country's finest weirdest sweetener: glucose isomerase, sulfuric acid, alpha amylase, and more (those enzymes are used to convert the glucose to fructose). It's not that hard to make: basically, just combine everything in the kit besides the glucose isomerase, strain through cheesecloth, heat, add glucose isomerase, boil, and cool. Weinstein went over to the Bon Appetit offices to demonstrate her kit, and, interestingly, it was a hit with the editors there. Before it's filtered to remove its yellow color and much of its flavor, it "tastes like corn candy," according to the editor of Bon Appetit's site. The filtering Continue reading >>

Catalytic Efficiency Of Immobilized Glucose Isomerase In Isomerization Of Glucose To Fructose [2008]

Catalytic Efficiency Of Immobilized Glucose Isomerase In Isomerization Of Glucose To Fructose [2008]

Catalytic efficiency of immobilized glucose isomerase in isomerization of glucose to fructose This translation tool is powered by Google. FAO is not responsible for the accuracy of translations. Catalytic efficiency of immobilized glucose isomerase in isomerization of glucose to fructose [2008] Catalytic efficiency of immobilized glucose isomerase in isomerization of glucose to fructose Glucose isomerase (GI) from Streptomyces rubiginosus was immobilized covalently onto Eupergit C 250L made by copolymerization of N,N-methylene-bis-methacrylamide, glycidyl methacrylate, allyl glycidyl ether and methacrylamide. The catalytic efficiency of immobilized GI in isomerization of glucose to fructose was found as three fold higher than that of free GI. The residual activity of immobilized GI after 18 reuses in a batch type stirred reactor was about 85% of its initial activity. The thermal stability of immobilized GI was almost same with that of the free GI at 60C for 18h preincubation time. The residual activities of immobilized GI when stored at 5C and 25C for four weeks were 72% and 69% of the initial activity, respectively. However, free GI retained 88% and 78% of its initial activity at 5C and 25C upon four weeks storage, respectively. Thus, the use of Eupergit C 250L immobilized GI instead of free GI is suggested in enzymatic isomerization of glucose to fructose. [isomerases, glucose, isomerization, temporal variation, glucose isomerase, Streptomyces rubiginosus, food additives, fructose, storage time, enzyme activity, storage conditions, immobilized enzymes, storage temperature, enzymatic treatment] Glucose isomerase (GI) from Streptomyces rubiginosus was immobilized covalently onto Eupergit C 250L made by copolymerization of N,N-methylene-bis-methacrylamide, glycidyl meth Continue reading >>

Xylose Isomerase - Wikipedia

Xylose Isomerase - Wikipedia

D-Xylose isomerase tetramer from Streptomyces rubiginosus PDB 2glk . [1] One monomer is coloured by secondary structure to highlight the TIM barrel architecture. In enzymology , a xylose isomerase ( EC 5.3.1.5 ) is an enzyme that catalyzes the interconversion of D-xylose and D-xylulose . This enzyme belongs to the family of isomerases , specifically those intramolecular oxidoreductases interconverting aldoses and ketoses . The isomerase has now been observed in nearly a hundred species of bacteria. Xylose -isomerases are also commonly called fructose-isomerases due to their ability to interconvert glucose and fructose. The systematic name of this enzyme class is D-xylose aldose-ketose-isomerase. Other names in common use include D-xylose isomerase, D-xylose ketoisomerase, and D-xylose ketol-isomerase. The activity of D-xylose isomerase was first observed by Mitsuhashi and Lampen in 1953 in the bacterium Lactobacillus pentosus. [2] Artificial production through transformed E.coli have also been successful. [3] In 1957, the D-xylose isomerase activity on D-glucose conversion to D-fructose was noted by Kooi and Marshall. [4] It is now known that isomerases have broad substrate specificity. Most pentoses and some hexoses are all substrates for D-xylose isomerase. Some examples include: D-ribose, L-arabinose, L-rhanmose, and D-allose. [5] Conversion of glucose to fructose by xylose isomerase was first patented in the 1960s, however, the process was not industrially viable as the enzymes were suspended in solution, and recycling the enzyme was problematic. [5] An immobile xylose isomerase that was fixed on a solid surface was first developed in Japan by Takanashi. [5] These developments were essential to the development of industrial fermentation processes used in manufactur Continue reading >>

Kinetics Of Glucose Isomerization To Fructose By Immobilized Glucose Isomerase: Anomeric Reactivity Of D-glucose In Kinetic Model

Kinetics Of Glucose Isomerization To Fructose By Immobilized Glucose Isomerase: Anomeric Reactivity Of D-glucose In Kinetic Model

Volume 84, Issue 2 , 30 November 2000, Pages 145-153 Kinetics of glucose isomerization to fructose by immobilized glucose isomerase: anomeric reactivity of d-glucose in kinetic model Author links open overlay panel Han SeungLee JuanHong Get rights and content The substrate specificity of immobilized d-glucose isomerase (EC 5.3.1.5) is investigated with an immobilized enzyme-packed reactor. A series of isomerization experiments with -, -, and equilibrated d-glucose solutions indicates that anomer as well as anomer is a substrate of the glucose isomerase at pH 7.5 and 60C. For substrate concentration of 0.028 mol l1 (1% w/v), the initial conversion rate of -d-glucose was 43% higher than that with equilibrated glucose at the same concentration and 113% higher than -d-glucose conversion rate. This anomeric reactivity of glucose isomerase is mathematically described with a set of kinetic equations based on the reaction steps complying with Briggs-Haldane mechanism and the experimentally determined kinetic constants. The proposed reaction mechanism includes the mutarotation and the isomerization reactions of - and -d-glucose with different rate constants. Continue reading >>

Kinetics Of Glucose Isomerization To Fructose By Immobilized Glucose Isomerase In The Presence Of Substrate Protection

Kinetics Of Glucose Isomerization To Fructose By Immobilized Glucose Isomerase In The Presence Of Substrate Protection

, Volume 18, Issue1 , pp 2733 | Cite as Kinetics of glucose isomerization to fructose by immobilized glucose isomerase in the presence of substrate protection The activity of immobilized glucose isomerase of Streptomyces murinus has been tested batchwise under different conditions in order to gather the related kinetic parameters necessary to optimize an immobilized enzyme column for the continuous production of high fructose corn syrup (HFCS). To this purpose, the Briggs-Haldane model incorporating an apparent first-order inactivation constant has been used with success. A comparison of the equilibrium constants and of the maximum theoretical conversion yields calculated at different temperatures with those estimated for the native enzyme demonstrates that the immobilization favours the transformation of glucose to fructose only at T > 70 C, as a possible consequence of a combined effect of catalysis and equilibrium thermodynamics enhancement. Enzyme inactivation has also been tested at different temperatures and sugar concentrations to evaluate the related kinetic parameters under different conditions of substrate protection. ImmobilizationFructoseStreptomycesImmobilize EnzymeIsomerase These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves. Continue reading >>

Glucose-to-fructose Conversion At High Temperatures With Xylose (glucose) Isomerases From Streptomyces Murinus And Two Hyperthermophilic Thermotoga Species.

Glucose-to-fructose Conversion At High Temperatures With Xylose (glucose) Isomerases From Streptomyces Murinus And Two Hyperthermophilic Thermotoga Species.

Department of Chemical Engineering, North Carolina State University, Stinson Drive, Box 7905, Raleigh, North Carolina 27695-7905, USA. The conversion of glucose to fructose at elevated temperatures, as catalyzed by soluble and immobilized xylose (glucose) isomerases from the hyperthermophiles Thermotoga maritima (TMGI) and Thermotoga neapolitana 5068 (TNGI) and from the mesophile Streptomyces murinus (SMGI), was examined. At pH 7.0 in the presence of Mg(2+), the temperature optima for the three soluble enzymes were 85 degrees C (SMGI), 95 degrees to 100 degrees C (TNGI), and >100 degrees C (TMGI). Under certain conditions, soluble forms of the three enzymes exhibited an unusual, multiphasic inactivation behavior in which the decay rate slowed considerably after an initial rapid decline. However, the inactivation of the enzymes covalently immobilized to glass beads, monophasic in most cases, was characterized by a first-order decay rate intermediate between those of the initial rapid and slower phases for the soluble enzymes. Enzyme productivities for the three immobilized GIs were determined experimentally in the presence of Mg(2+). The highest productivities measured were 750 and 760 kg fructose per kilogram SMGI at 60 degrees C and 70 degrees C, respectively. The highest productivity for both TMGI and TNGI in the presence of Mg(2+) occurred at 70 degrees C, pH 7.0, with approximately 230 and 200 kg fructose per kilogram enzyme for TNGI and TMGI, respectively. At 80 degrees C and in the presence of Mg(2+), productivities for the three enzymes ranged from 31 to 273. A simple mathematical model, which accounted for thermal effects on kinetics, glucose-fructose equilibrium, and enzyme inactivation, was used to examine the potential for high-fructose corn syrup (HFCS) pro Continue reading >>

Us4308349a - Isomerization Of Glucose To Fructose Using Glucose Isomerase From Ampullariella - Google Patents

Us4308349a - Isomerization Of Glucose To Fructose Using Glucose Isomerase From Ampullariella - Google Patents

US4308349A - Isomerization of glucose to fructose using glucose isomerase from ampullariella - Google Patents Isomerization of glucose to fructose using glucose isomerase from ampullariella US4308349A US05884925 US88492578A US4308349A US 4308349 A US4308349 A US 4308349A US 05884925 US05884925 US 05884925 US 88492578 A US88492578 A US 88492578A US 4308349 A US4308349 A US 4308349A Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.) Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.) C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING C12R1/01Processes using microorganisms using bacteria or actinomycetales C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes C12N9/92Glucose isomerase (5.3.1.5; 5.3.1.9; 5.3.1.18) C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS

High-fructose Corn Syrups (hfcs)

High-fructose Corn Syrups (hfcs)

With the development of glucoamylase in the 1940s and 1950s it became a straightforward matter to produce high DE glucose syrups. However, these have shortcomings as objects of commerce: D-glucose has only about 70% of the sweetness of sucrose, on a weight basis, and is comparatively insoluble. Batches of 97 DE glucose syrup at the final commercial concentration (71% (w/w)) must be kept warm to prevent crystallisation or diluted to concentrations that are microbiologically insecure. Fructose is 30% sweeter than sucrose, on a weight basis, and twice as soluble as glucose at low temperatures so a 50% conversion of glucose to fructose overcomes both problems giving a stable syrup that is as sweet as a sucrose solution of the same concentration (see Table 4.3 ). The isomerisation is possible by chemical means but not economical, giving tiny yields and many by-products (e.g. 0.1 M glucose 'isomerised' with 1.22 M KOH at 5C under nitrogen for 3.5 months gives a 5% yield of fructose but only 7% of the glucose remains unchanged, the majority being converted to various hydroxy acids). One of the triumphs of enzyme technology sofar has been the development of 'glucose isomerase'. Glucose is normallyisomerised to fructose during glycolysis but both sugars are phosphorylated. Theuse of this phosphohexose isomerase may be ruled out as a commercial enzymebecause of the cost of the ATP needed to activate the glucose and because twoother enzymes (hexokinase and fructose-6-phosphatase) would be needed tocomplete the conversion. Only an isomerase that would use underivatised glucoseas its substrate would be commercially useful but, until the late 1950s, theexistence of such an enzyme was not suspected. At about this time, enzymes werefound that catalyse the conversion of D-xylose to an Continue reading >>

Immobilization Of Recombinant Glucose Isomerase For Efficient Production Of High Fructose Corn Syrup.

Immobilization Of Recombinant Glucose Isomerase For Efficient Production Of High Fructose Corn Syrup.

Appl Biochem Biotechnol. 2017 Sep;183(1):293-306. doi: 10.1007/s12010-017-2445-0. Epub 2017 Mar 11. Immobilization of Recombinant Glucose Isomerase for Efficient Production of High Fructose Corn Syrup. Key Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, 310014, People's Republic of China. Engineering Research Center of Bioconversion and Biopurification of Ministry of Education, Zhejiang University of Technology, Hangzhou, 310014, People's Republic of China. Zhejiang Huakang Pharmaceutical Co., Ltd., 18 Huagong Road, Huabu Town, 324302, Kaihua, People's Republic of China. Key Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, 310014, People's Republic of China. [email protected] Engineering Research Center of Bioconversion and Biopurification of Ministry of Education, Zhejiang University of Technology, Hangzhou, 310014, People's Republic of China. [email protected] Glucose isomerase is the important enzyme for the production of high fructose corn syrup (HFCS). One-step production of HFCS containing more than 55% fructose (HFCS-55) is receiving much attention for its industrial applications. In this work, the Escherichia coli harboring glucose isomerase mutant TEGI-W139F/V186T was immobilized for efficient production of HFCS-55. The immobilization conditions were optimized, and the maximum enzyme activity recovery of 92% was obtained. The immobilized glucose isomerase showed higher pH, temperature, and operational stabilities with a K m value of 272mM and maximum reaction rate of 23.8mMmin-1. The fructose concentration still retained above 55% after the immobilized glucose Continue reading >>

Glucose Isomerase Production By Penicillium Fellutanum Isolated From Mangrove Sediment

Glucose Isomerase Production By Penicillium Fellutanum Isolated From Mangrove Sediment

Glucose Isomerase Production by Penicillium fellutanum Isolated from Mangrove Sediment Effects of pH, temperature, mineral salts, incubation time, sources and concentrations of carbon and nitrogen were tested in submerged fermentation process in production of glucose isomerase by Penicillium fellutanum isolated from coastal mangrove soil. The production medium prepared in distilled water, supplemented with 0.1% mineral salts, 1.5% xylose ( carbon source ), 1% yeast extract (nitrogen source), maintained with pH of 6.5 and incubated at 30C for 120 h was found optimal for production of glucose isomerase. How to cite this article: K. Kathiresan and S. Manivannan, 2006. Glucose Isomerase Production by Penicillium fellutanum Isolated from Mangrove Sediment. Trends in Applied Sciences Research, 1: 524-528. URL: With ever increasing demand for sugar and its rising price, considerable effort has been made during the past decade to find alternative sweetener. The production of sweetener from corn starch by microbial saccharides is an important application of enzyme technology in the food industry (Mermelstein, 1975; Aunstrup et al., 1979). The present study for high fructose corn syrup production involves several separate enzymatic steps, including liquification by amylase, saccharification by gluco-amylase and isomeraization by glucose isomerase. Of these, Glucose isomerase is an important one, which is an intracellular enzyme found in microbes which can utilise xylose as a carbon source for growth (Chen, 1980a). Physiological function of the enzyme is isomerization of D-xylose to D-xylulose in vivo and conversion of D-glucose to D-fructose in vitro (Bok et al., 1984). Activity of the enzyme also depends on reaction conditions (i.e., temperature, pH and metal cofactor) (Antrim Continue reading >>

21 Cfr 184.1372 - Insoluble Glucose Isomerase Enzyme Preparations.

21 Cfr 184.1372 - Insoluble Glucose Isomerase Enzyme Preparations.

21 CFR 184.1372 - Insoluble glucose isomerase enzyme preparations. 184.1372 Insoluble glucose isomerase enzyme preparations. (a) Insoluble glucose isomerase enzyme preparations are used in the production of high fructose corn syrup described in 184.1866 . They are derived from recognized species of precisely classified nonpathogenic and nontoxicogenic microorganisms , including Streptomyces rubiginosus, Actinoplanes missouriensis, Streptomyces olivaceus, Streptomyces olivochromogenes, and Bacillus coagulans, that have been grown in a pure culture fermentation that produces no antibiotics. They are fixed (rendered insoluble) for batch production with GRAS ingredients or may be fixed for further immobilization with either GRAS ingredients or materials approved under 173.357 of this chapter. (b) The ingredient meets the general and additional requirements for enzyme preparations in the Food Chemicals Codex, 3d Ed. (1981), p. 107, which is incorporated by reference. Copies are available from the National Academy Press, 2101 Constitution Ave. NW., Washington, DC 20418, or available for inspection at the National Archives and Records Administration (NARA). For information on the availability of this material at NARA, call 202-741-6030, or go to: (c) In accordance with 184.1(b)(1) , the ingredient is used in food with no limitation other than current good manufacturing practice. The affirmation of this ingredient as generally recognized as safe (GRAS) as a direct human food ingredient is based upon the following current good manufacturing practice conditions of use: (1) The ingredient is used as an enzyme, as defined in 170.3(o)(9) of this chapter, to convert glucose to fructose. (2) The ingredient is used in high fructose corn syrup, at levels not to exceed current good manu Continue reading >>

Optimization Of Fermentation Medium For The Production Of Glucose Isomerase Using Streptomyces Sp. Sb-p1

Optimization Of Fermentation Medium For The Production Of Glucose Isomerase Using Streptomyces Sp. Sb-p1

Optimization of Fermentation Medium for the Production of Glucose Isomerase Using Streptomyces sp. SB-P1 1Department of Biosciences, Maharaja Ranjit Singh College of Professional Sciences, Madhya Pradesh, Indore 452001, India 2Department of Life Sciences, Gujarat University, Gujarat, Ahmedabad 380009, India Received 27 March 2012; Accepted 14 May 2012 Copyright 2012 Sheetal Bhasin and H. A. Modi. This is an open access article distributed under the Creative Commons Attribution License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The combination of medium ingredients has a profound influence on the metabolic pathways running in the microorganism which regulates the production of numerous metabolites. Glucose isomerase (GI), an enzyme with huge potential in the market, can isomerise glucose into fructose. GI is used widely for the production of High-Fructose Corn Syrup (HFCS). HFCS is used as a sweetener in food and pharmaceutical industries. Streptomyces are well-known producers of numerous enzymes including glucose isomerase. An array of 75 isolates was screened for the production of glucose isomerase. The isolate Streptomyces sp. SB-P1 was found to produce maximum amount of extracellular GI. Sucrose and raffinose among pure carbon sources and corn cob and wheat husk among crude agro residues were found to yield high enzyme titers. Potassium nitrate among pure nitrogen sources and soy residues among crude sources gave maximum production. Quantitative effect of carbon, nitrogen, and inducer on GI was also determined. Plackett-Burman design was used to study the effect of different medium ingredients. Sucrose and xylose as carbon sources and peptone and soy residues as nitrogen sources prove Continue reading >>

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