Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.15 (pectinase)
2,440 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Dried distillers' grains with solubles (DDGS), a co-product of corn ethanol production, was investigated as a feedstock for additional ethanol production. DDGS was pretreated with liquid hot-water (LHW) and ammonia fiber explosion (AFEX) processes. Cellulose was readily converted to glucose from both LHW and AFEX treated DDGS using a mixture of commercial cellulase and beta-glucosidase; however, these enzymes were ineffective at saccharifying the xylan present in the pretreated DDGS. Several commercial enzyme preparations were evaluated in combination with cellulase to saccharify pretreated DDGS xylan and it was found that adding commercial grade (e.g. impure) pectinase and feruloyl esterase (FAE) preparations were effective at releasing arabinose and xylose. The response of sugar yields for pretreated AFEX and LHW DDGS (6wt%/solids) were determined for different enzyme loadings of FAE and pectinase and modeled as a response surfaces. Arabinose and xylose yields rose with increasing FAE and pectinase enzyme dosages for both pretreated materials. When hydrolyzed at 20wt%/solids with the same blend of commercial enzymes, the yields were 278 and 261g sugars (i.e. total of arabinose, xylose, and glucose) per kg of DDGS (dry basis, db) for AFEX and LHW pretreated DDGS, respectively. The pretreated DDGS's were also evaluated for fermentation using Saccharomyces cerevisiae at 15wt%/solids. Pretreated DDGS were readily fermented and were converted to ethanol at 89-90% efficiency based upon total glucans; S. cerevisiae does not ferment arabinose or xylose.
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PMID:Enzyme characterization for hydrolysis of AFEX and liquid hot-water pretreated distillers' grains and their conversion to ethanol. 1799 46

After observing the effects of purified cellulase (C), hemicellulase (H), pectinase (P), and their combinations on the in vitro digestibility of a corn-soybean meal broiler diet, we examined the associations between pectin breakdown and the digestibilities of CP and DM by using free galacturonic acid (GA) as an index of pectin breakdown. There was no significant effect of the single enzymes except for H. However, the enzyme combinations H + P, C + H, and C + H + P significantly increased CP and DM digestibilities, whereas the combination of C + P was not effective. Because H has activities of both H and P, these enzymes were considered to be important in stimulating digestion. Furthermore, when the enzymes increased CP and DM digestibilities, GA concentration was significantly higher, and clear correlations between CP and DM digestibilities and GA concentration were observed, whereas correlations between the digestibilities and concentration of glucose or xylose + mannose as indices of cellulose and hemicellulose breakdown, respectively, were not significant. From these observations, we hypothesized that a mixture of enzymes could increase the protein digestibility of broiler feed. Thus, in the in vivo experiment, low-protein (19% CP) diets made mainly of corn and soybean meal with or without mixed enzymes were prepared and given to broiler chicks. The birds given the diet containing mixed enzymes showed significantly higher BW gain, with higher CP and DM digestibilities than the birds given the diet without the mixed enzymes. Moreover, the growth rate was same as that of the birds given the normal (21% CP) diet. The results indicate that the mixed enzyme preparation can effectively degrade indigestible cell constituents and thus enable the protein of the broiler feed to become more digestible. Furthermore, the results indicate the importance of H as a rate-limiting factor of cell wall breakdown.
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PMID:An effective combination of carbohydrases that enables reduction of dietary protein in broilers: importance of hemicellulase. 1833 93

An alkali extract of cell walls of Gossypium hirsutum L. was sequentially digested by endo-polygalacturonase (EC 3.2.1.15), arabinofuranosidase AN1571.2 (EC 3.2.1.55), endo-arabinase (EC 3.2.1.99), and rhamnogalacturonan hydrolase AN9314.2 (EC 3.2.1.15). The rhamnogalacturonan hydrolase-generated oligosaccharides were separated by ultrafiltration, size-exclusion, and anion exchange chromatography. Fractions from the anion exchange chromatography were pooled, lyophilized, and screened by MALDI-TOFMS. A new oligosaccharide (RGS29), which contained a rhamnogalacturonan dimer backbone with two galactose and two arabinose residues in the side chains, was found. Its structure was identified by 1D and 2D NMR spectra as follows: [Formula: see text].
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PMID:Isolation and structural characterization of a novel oligosaccharide from the rhamnogalacturonan of Gossypium hirsutum L. 1835 94

Microsomal membranes from etiolated wheat (Triticum aestivum) seedlings cooperatively incorporated xylose (Xyl), arabinose, and glucuronic acid residues from their corresponding uridine 5'-diphosphosugars into an ethanol-insoluble glucurono(arabino)xylan (GAX)-like product. A glucuronyltransferase activity that is enhanced by the presence of UDP-Xyl was also identified in these microsomes. Wheat glucuronyltransferase activity was optimal at pH 7 and required manganese ions, and several lines of evidence suggest its involvement in GAX-like biosynthesis. The GAX characteristics of the 14C-product were confirmed by digestion with a purified endo-xylanase from Aspergillus awamori (endo-xylanase III) and by total acid hydrolysis, resulting in a Xyl:arabinose:glucuronic acid molar ratio of approximately 105:34:1. Endo-xylanase III released only three types of oligosaccharides in addition to free Xyl. No radiolabel was released as xylobiose, xylotriose, or xylotetraose, indicating the absence of long stretches of unbranched Xyl residues in the nascent GAX-like product. High-pH anion exchange chromatography analysis of the resulting oligosaccharides along with known arabinoxylan oligosaccharide standards suggests that a portion of the nascent GAX-like product has a relatively regular structure. The other portion of the [14C]GAX-like polymer was resistant to proteinase K, endo-polygalacturonase, and endo-xylanase III (GH11 family) but was degraded by Driselase, supporting the hypothesis that the xylan backbone in this portion of the product is most likely highly substituted. Size exclusion chromatography indicated that the nascent GAX-like polymer had an apparent molecular mass of approximately 10 to 15 kD; however, mature GAXs from wheat cell walls had larger apparent molecular masses (>66 kD).
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PMID:UDP-Xylose-stimulated glucuronyltransferase activity in wheat microsomal membranes: characterization and role in glucurono(arabino)xylan biosynthesis. 1835 44

A washed carrot substrate, prepared with high yields and easy handling properties, was found to be a suitable substrate for studying cellulolytic and pectinolytic degradation processes. A cellulase from Trichoderma reesei, and Rohament P, a macerating enzyme from Aspergillus alleaceus in endopolygalacturonase, degraded the washed carrot substrate to an extent of 60%. With the combined action of both enzymes, degradation was more than 80%. Simultaneous action of both enzymes was more efficient than their sequential use. The effect of temperature, pH, incubation time, enzyme concentration, and substrate concentration on the degradation by the single enzymes and their mixture were studied. Gas chromatographic sugar analysis revealed that Rohament P liberated glucose, arabinose, and galactose in the low-molecular-weight fraction obtained by ultrafiltration, in addition to high amounts of galacturonic acid. These carbohydrates were also found in the high-molecular-weight fraction (retentate) together with rhamnose and mannose. Cellulase BC released mainly glucose, although galacturonic acid, arabinose, xylose, and mannose were also detected both in the ultrafiltrate and retentate. Morphologically, during Rohament P degradation of the washed carrot substrate, damaged tissues and disintegrated cells were seen, whereas on cellulase BC action mainly disintegrated cell walls were observed.
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PMID:Degradation of a washed carrot preparation by cellulases and pectinases. 1855 48

Polysaccharide extracts were obtained from chestnut bran (Castanea sativa), grape marc (Vitis vinifera) and apple marc (Malus spp.) and fractionated by size exclusion chromatography after endopolygalacturonase degradation. Compositional and linkage analyses by GC and GC-MS showed the characteristic rhamnogalacturonan structure with specific arabinan (apple marc) and type II arabinogalactan (chestnut bran, grape marc) side chains. Type II arabinogalactan rhamnogalacturonan from chestnut bran significantly stimulated the in vitro differentiation of human keratinocytes, giving evidence of a tight structure-function relationship. This molecule comprises short and ramified 3- and 3,6-beta- D-galactan and 5- and 3,5-alpha-L-arabinan side chains, but also contains significant amounts of t-Xyl and 4-Xyl with a characteristic 2:1 ratio. Enzymatic hydrolysis of this polysaccharide produced fragments of lower molecular weight with unchanged xylose content which conserved the same ability to stimulate human keratinocyte differentiation. It could be then speculated that dimeric xylosyl-xylose and/or longer oligomeric xylose side chains attached to a galacturonan and closely associated to hairy rhamno-galacturonan domains are essential patterns that could determine the biological activity of pectins.
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PMID:Structural patterns of rhamnogalacturonans modulating Hsp-27 expression in cultured human keratinocytes. 1856 Mar 39

The Malian medicinal plant Biophytum petersianum Klotzsch (Oxalidaceae) is used as a treatment against various types of illnesses related to the immune system, such as joint pains, inflammations, fever, malaria, and wounds. A pectic polysaccharide obtained from a hot water extract of the aerial parts of B. petersianum has previously been reported to consist of arabinogalactans types I and II (AG-I and AG-II), probably linked to a rhamnogalacturonan backbone. We describe here further structural characteristics of the main polysaccharide fraction (BP1002) and fractions obtained by enzymatic degradations using endo-alpha-d-(1-->4)-polygalacturonase (BP1002-I to IV). The results indicate that in addition to previously reported structures, rhamnogalacturan type II and xylogalacturonan areas appear to be present in the pectic polymer isolated from the plant. Atomic force microscopy confirmed the presence of branched structures, as well as a polydisperse nature. We further tested whether the BP1002 main fraction or the enzymatically degraded products could induce immunomodulating activity through stimulation of subsets of leukocytes. We found that macrophages and dendritic cells were activated by BP1002 fractions, while there was little response of T cells, B cells, and NK cells. The enzymatic treatment of the BP1002 main fraction gave important information on the structure-activity relations. It seems that the presence of rhamnogalacturonan type I is important for the bioactivity, as the bioactivity decreases with the decreased amounts of rhamnose, galactose, and arabinose. The demonstration of bioactivity by the plant extracts might indicate the mechanisms behind the traditional medical use of the plant.
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PMID:Pectic polysaccharides from Biophytum petersianum Klotzsch, and their activation of macrophages and dendritic cells. 1880 20

Okra pods are commonly used in Asia as a vegetable, food ingredient, as well as a traditional medicine for many different purposes; for example, as diuretic agent, for treatment of dental diseases and to reduce/prevent gastric irritations. The healthy properties are suggested to originate from the high polysaccharide content of okra pods, resulting in a highly viscous solution with a slimy appearance when okra is extracted with water. In this study, we present a structural characterisation of all major cell wall polysaccharides originating from okra pods. The sequential extraction of okra cell wall material yielded fractions of soluble solids extractable using hot buffer (HBSS), chelating agent (CHSS), dilute alkaline (DASS) and concentrated alkaline (CASS). The HBSS fraction was shown to be rich in galactose, rhamnose and galacturonic acid in the ratio 1.3:1:1.3. The degree of acetylation is relatively high (DA=58) while the degree of methyl esterification is relatively low (DM=24). The CHSS fraction contained much higher levels of methyl esterified galacturonic acid residues (63% galacturonic acid; DM=48) in addition to minor amounts of rhamnose and galactose. The ratio of galactose to rhamnose to galacturonic acid was 1.3:1.0:1.3 and 4.5:1.0:1.2 for HBSS and CHSS, respectively. These results indicated that the HBSS and CHSS fractions contain rhamnogalacturonan type I next to homogalacturonan, while the latter is more prevailing in CHSS. Also the DASS fraction is characterised by high amounts of rhamnose, galactose, galacturonic acid and some arabinose, indicating that rhamnogalacturonan I elements with longer arabinose- and galactose-rich side chains were part of this fraction. Partial digestion of HBSS and CHSS by pectin methyl esterase and polygalacturonase resulted in a fraction with a lower Mw and lower viscosity in solution. These samples were subjected to NMR analysis, which indicated that, in contrast to known RG I structure, the acetyl groups in HBSS are not located on the galacturonic acid residues, while for CHSS only part of the acetyl groups are located on the RG I galacturonic acid residues. The CASS fraction consisted of XXXG-type xyloglucan and 4-methylglucuronoxylan as shown by their sugar (linkage) composition and enzymatic digestion.
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PMID:Characterisation of cell wall polysaccharides from okra (Abelmoschus esculentus (L.) Moench). 1906 90

To enhance the conversion of the cellulose and hemicellulose, the corncob pretreated by aqueous ammonia soaking was hydrolyzed by enzyme complexes. The saturation limit for cellulase (Spezyme CP) was determined as 15 mg protein/g glucan (50 filter paper unit (FPU)/g glucan). The accessory enzymes (beta-glucosidase, xylanase, and pectinase) were supplemented to hydrolyze cellobiose (cellulase-inhibiting product), hemicellulose, and pectin (the component covering the fiber surfaces), respectively. It was found that beta-glucosidase (Novozyme 188) loading of 1.45 mg protein/g glucan [30 cellobiase units (CBU)/g glucan] was enough to eliminate the cellobiose inhibitor, and 2.9 mg protein/g glucan (60 CBU/g glucan) was the saturation limit. The supplementation of xylanase and pectinase can increase the conversion of cellulose and hemicellulose significantly. The yields of glucose and xylose enhanced with the increasing enzyme loading, but the increasing trend became low at high loading. Compared with xylanase, pectinase was more effective to promote the hydrolysis of cellulose and hemicellulose. The supplementation of pectinase with 0.12 mg protein/g glucan could increase the yields of glucose and xylose by 7.5% and 29.3%, respectively.
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PMID:Enhanced enzymatic hydrolysis of lignocellulose by optimizing enzyme complexes. 1928 67

Cassava pulp, a solid by-product from starch processing, is a promising and underused biomass that can be converted to biofuels and other value-added bio-products. In this study, an alternative cassava pulp saccharification process, which utilizes the multi-activity enzyme from Aspergillus niger BCC17849 and obviates the need for a pre-gelatinization step, was developed. The crude multi-enzyme composed of non-starch polysaccharide hydrolyzing enzyme activities, including cellulase, pectinase and hemicellulase act cooperatively to release the trapped starch granules from the fibrous cell wall structure for subsequent saccharification by raw starch degrading activity. A high yield of fermentable sugars, equivalent to 716 mg glucose and 67 mg xylose/g of cassava pulp, was obtained after 48 h incubation at 40 degrees C and pH 5 using the multi-enzyme, which was greater than the yield obtained from the optimized combinations of the corresponding commercial enzymes. The multi-enzyme saccharification reaction can be performed simultaneously with the ethanol fermentation process using a thermotolerant yeast Candida tropicalis BCC7755. The combined process produced 14.3 g/l ethanol from 4% (w/v) cassava pulp after 30 h of fermentation. The productivity rate of 0.48 g/l/h is equivalent to 93.7% of the theoretical yield based on total starch and cellulose, or 85.4% based on total fermentable sugars. The non-thermal enzymatic saccharification process described is more energy efficient and yields more fermentable sugar than the conventional enzymatic process. Furthermore, the process is applicable for production of various bio-products of economic importance.
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PMID:Simultaneous non-thermal saccharification of cassava pulp by multi-enzyme activity and ethanol fermentation by Candida tropicalis. 1939 45


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