How is isomerase used in the creation of slimming foods

All these strategies either isolated or preferably suitably integrated have been put into practice in food and feed, to improve existing processes or to implement new ones, with the latter often combined with the output of new goods, resulting from novel enzymatic activities.

Given the recent developments in this field, this trend is foreseen to be further implemented. National Center for Biotechnology Information , U. Journal List Enzyme Res v. Enzyme Res. Published online Sep Author information Article notes Copyright and License information Disclaimer. Received Jul 7; Accepted Sep 1. 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.

This article has been cited by other articles in PMC. Abstract Food and feed is possibly the area where processing anchored in biological agents has the deepest roots. Introduction Food processing through the use of biological agents is historically a well-established approach. Relevant Enzymes: Tapping for Improved Biocatalysts 2. General Aspects and the Screening Approach Roughly all classes of enzymes have an application within the food and feed area, but hydrolases are possibly the prevalent one.

Table 1 An overview of enzymes used in food and feed processing adapted from [ 10 , 12 , 13 , 68 ]. Open in a separate window. Table 2 Some examples of strategies undertaken to improve the performance of enzymes with applications in food and feed. After 3 rounds the mutant enzyme from S. Enhanced activities are maintained between pH 6.

The resulting mutant displayed a 3-fold increase in catalytic efficiency with L-arabinose as substrate. Table 3 Examples of enzymes isolated from various marine higher organisms with potential of application in food and feed adapted from [ 68 , 69 ].

Class Enzyme Source Transferases Transglutaminase Muscles of atka mackerel Pleurogrammus azonus , botan shrimp Pandalus nipponensis , carp Cyprinus carpio , rainbow trout Oncorhynchus mykiss , scallop Patinopecten yessoensis. Chymotrypsin Atlantic cod Gadus morhua , crayfish, white shrimp.

Pepsin Arctic capelin Mallotus villosus , Atlantic cod Gadus morhua. Mangrove crab Scylla serrata , found in estuaries and mangroves of Africa, Asia and Australia.

Sardine Orange roughy Hoplostethus atlanticus. Improving Biocatalysts: Beyond Screening Taking advantage of the knowledge gathered on molecular biology, high-throughput processing, and computer-assisted design of proteins, in-vitro improvement of biocatalysts have been consistently implemented [ 90 — 93 ].

The alterations promoted are performed based on the growing knowledge on the structure and functions of enzyme. Information on this matter mostly comes from bioinformatics, which provides data on amino-acid propensities and on protein sequences. Adequate processing of the data enable the output of generalized rules predicting the effect of mutations on enzyme properties. Also used are molecular potential functions, which, once implemented, enable the prediction of the effect of mutations in enzyme structure [ 97 ].

Computational tools used for enzyme engineering have been recently reviewed [ ]. Enzyme engineering through molecular simulations requires structural data from the native enzyme, which can be preferably obtained from crystallography or NMR.

Otherwise a model is built based on known enzyme structures with homologous sequences [ 90 ]. Computational methods are also welcome in directed evolution, as a tool to better lead the random mutagenesis [ 97 ]. Ultimately this approach is put into practice by producing a site-directed mutant, where selected amino acids are replaced with those suggested from the outcome of modeling.

Some relevant examples of this strategy in the area of food and feed processing are given. Immobilization There are several issues that can be lined up to sustain enzyme immobilization.

Table 4 A generalized characterization of immobilization methods. Typical Bioreactors The most common form of enzymatic reactors for continuous operation is the packed-bed setup, basically a cylindrical column holding a fixed bed of catalyst particles Figure 1. Figure 1. References 1. Vasic-Racki D. History of industrial biotransformations—dreams and realities. Industrial Biotransformations. History of enzymology with emphasis on food production. Handbook of Food Enzymology. Enzymes for technical applications.

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Fundamentals and Applications. Applied biocatalysis: an overview. Upload document Create flashcards. Flashcards Collections. Documents Last activity. Add to Add to collection s Add to saved. Sovan Ponna Mr. There are proving that people want to be skinnier and they think that it is not right and that people will see them differently. For example some people that are in my family always eat very little, they eat yogurt, and eat a lot of vegetable, eating vegetable is good but sometimes you need more proteins.

Using slimming food can make you skinnier and you can eat a bit more food. The enzyme that I am going to talk about is Isomerase , this enzyme turns glucose into fructose. The industrial that I am going to talking is slimming food.

This two fit each other really well because slimming uses fructose because it is very sweet and it have very little calories. The enzyme that can make glucose is Isomerase, so slimming food and my enzyme fits each other really well. Not like other food, slimming food have fructose instead of glucose. Glucose and fructose are the same the only difference are that glucose has more calories than fructose but fructose is sweeter than glucose Watson BBC.

There is an enzyme that is called Isomerase; this enzyme is used to change glucose into fructose. We use fructose in slimming because since it is very sweet we can put a little amount of fructose; also it contains very little calories, which is why people use fructose for slimming food.

Wikipedia — Site for picture The slimming food solve the problem of people that are overweight, because since it has less calories and it is very sweet then people would really like it, and while they are using it, they will lose weight bit by bit. Niel Commons Biotechnology Essay but when you want to stop losing weight you can stop using it and from then on you can decide if you want to eat a lot or not. Houston et al. The most prevalent and best-studied PDIL protein is an ortholog of an approximately kD PDI that has been found in most eukaryotic organisms investigated, including plants [28] , [32].

Several physiological roles for PDI have been reported in plants. In rice, an esp2 endosperm storage protein 2 mutation caused loss of PDIL expression and accumulation of proglutelins, suggesting that PDIL retains glutelin precursors within the cisternal ER by chaperone activity, resulting in inhibition of abnormal aggregation of prolamin [30] , [31]. In addition, PDIL proteins have different activities in rice. In this study, we analyzed PDIL knock-out transgenic rice, and in particular, its seed.

To characterize seed properties such as an opaque endosperm and a thick aleurone layer, the amount and composition of seed proteins were identified by proteomic methods. Furthermore, inner seed factors such as starch granules, protein bodies, and free sugars were also examined. Here, we show that PDIL is a critical factor in seed development including in the development of the endosperm and aleurone layer through regulation of the proportion of various seed proteins including storage proteins.

T-DNA insertion mutant rice was generated from the cultivar Dongjinbyeo wild type according to a method previously described [33] , [34]. The same mutant lines were also examined by western blotting using an anti-PDIL antibody we previously generated [36]. Selected homozygote lines were used to produce progeny for this study.

Sample preparation was performed by the following method. Whole seeds chilled in liquid nitrogen were homogenized using a mortar and pestle. Then, the strips were immersed for 10 min in solution 50 mM Tris-Cl pH 6. After electrophoresis, gels were stained with silver nitrate as previously described [37].

From the stained gels, digitized images were acquired and quantitatively analyzed using the PDQuest version 7. The quantity of each spot was normalized by total valid spot intensity. Protein spots were enzymatically digested in-gel using modified porcine trypsin as previously described [38].

Peptides were evaporated with an N 2 laser at nm and accelerated with a 20 kV injection pulse for time-of-flight analysis. Each spectrum was a cumulative average of laser shots. To determine the confidence of identified proteins, the Z-score, MASCOT score, and sequence coverage were used as the determining criteria.

Distillation and titration were carried out automatically. Thereafter, total nitrogen content was measured, and the protein content was calculated by multiplying 6. Whole or sectioned seeds were used for staining with methylene blue.

Cross-sectioned seeds were immersed into 0. To investigate PDIL levels during seed development, total proteins were isolated from whole grains that were sampled at 5, 10, 20, 30, 40, and 50 days after flowering DAF. After electrophoresis, the proteins were transferred onto PVDF membrane, and detected as above. Total RNA was extracted from different developmental stages and tissues to investigate spatial and temporal expression patterns of PDIL according to a method previously described [39].

The primer sets used for these studies are listed in Table S2. Total RNA was isolated from whole grains that were sampled at 5, 10, 20, 30, 40, and 50 DAF as previously described [35].

Total RNA was separated by formaldehyde-agarose gel electrophoresis and transferred onto a nylon membrane Millipore. The powder was extracted with buffer 55 mM Tris-Cl pH 6. Purified starch was dried in air, coated with gold particles, and then finally observed by SEM.

Protein bodies were observed by transmission electron microscopy TEM. The samples were washed in 50 mM sodium cacodylate buffer and then distilled water and then stained with 0. After centrifuge, supernatant was filtered with a 0.

The X-ray diffraction patterns were analyzed as previously described [41]. The remaining seeds were also crushed, used and filtered as described above.

Selected clones were rescreened on media lacking leucine, tryptophan, and histidine with 5 mM 3-amino-1,2,4-triazole 3-AT. A phylogenetic tree was generated by the neighbor-joining method with 1, bootstrap replicates using MEGA5 software. In eukaryotic cells, most proteins are post-translationally modified after synthesis in the ER, with the formation and isomerization of disulfide bonds an important occurrence after translation.

R was provided by Dr. R were opened and removed. The mutants showed a chalky and uneven phenotype. Bar, 0. PDI can control the stability and activity of target proteins by regulating formation and isomerization of disulfide bonds. Interestingly, only sucrose synthase GT1 was highly up-regulated in the wild type. Next, to determine if any correlation exists between protein content and protein body or structure, we checked protein bodies in the sectioned endosperm by TEM.

We also measured the thickness of the aleurone layer by electron microscopy. Thus, to evaluate the effect of PDIL on aleurone layer development, we investigated the PDIL distribution in the outer part of the endosperm including the aleurone layer. This was done by western blot analysis using differently husked and milled grains Figure 3C. Abbreviations: vs, ventral side; ds, dorsal side. Bar, 1 mm left , and 0. C Dried seeds were polished to different extents. After detection, the membrane was stained with Coomassie brilliant blue right.

Examination of the same seeds using optical microscopy showed an opaque endosperm, particularly in the outer part of the endosperm Figure S4B , which is consistent with recently published data [43]. Previous results showed that the endosperm of the rice sugary-1 mutant EM remained white after staining with I2-KI solution, whereas other mutant types such as EM turned blue-black in non-waxy rice [12]. Furthermore, X-ray diffraction analysis revealed nearly the same diffraction area and peak pattern Figure S6.

Thus, the outer part of the endosperm was again examined by X-ray diffraction analysis. Previous reports show that the endosperms of several mutants have opaque phenotypes, which are caused by alterations in starch and amylose contents [14] , [44] , [45]. To understand the possible regulatory roles of PDIL protein during rice development, we investigated expression of the PDIL gene in leaf, root, stem, crown, and seed.

The results showed that PDIL was expressed in all tissues throughout mature developmental stages, although with varying levels of expression Figure 5A. Next, we checked the PDIL transcript levels during seed development in detail. Thus, to investigate whether PDIL stability or activity is post-translationally regulated, we performed 2-DE and identified protein spots with mass spectrometry.

The results showed that five different protein spots were identified as PDIL Figure 5D , Table S4 , suggesting that its stability or activity can be regulated by post-translational modification or processing. B Total RNA was isolated from developing seeds at the indicated time points and separated on formaldehyde-agarose gels. After electrophoresis, total RNA was transferred onto a nylon membrane. DAF, days after flowering. Total proteins were extracted from the wild type at the indicated time points.

After blotting, the membrane was stained with Coomassie brilliant blue right. D Proteomic analysis of rice seed proteins.

Total proteins were extracted from mature seeds of WT and then separated by 2-DE. The boxed region was enlarged right. Arrowheads indicate PDIL protein spots. Accumulating data suggest that PDIL protein can regulate many interacting partners. In addition, PDIL stability and activity may be regulated by other proteins.

We used an Arabidopsis library because a larger number of proteins are characterized in Arabidopsis compared to rice, which facilitates characterization of the function of the isolated proteins in rice. Next, we tried to isolate its homolog in rice. First, we checked the rice homologs by phylogenetic analysis.

However, as shown in the phylogenetic tree, there are still two other OsCP1 homologs that remained unidentified, Os05g and Os01g