• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.2
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• pp.242-246
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• 1995

This paper was carried out to investigate changes in cell wall, cell wall polysaccharides, pectic substances extracted from cell wall of persimmon fruits treated with polygalacturonase and $\beta$-galactosidase in vitro. Degrading degree of cell wall treated with cell wall-degrading enzymes were higher in order polygalacturonase, polygalacturonase+$\beta$-galactosidase and $\beta$-galactosidase. Contents of soluble pectic substances in cell wall treated with cell wall-degrading enzymes showed as the same order as degrading degree of cell wall, while contents of insoluble pectin lower. Contents of versene-soluble pectin and total pectic substance were not affected by cell wall-degrading enzymes. Contents of uronic acid and hexose in soluble material isolated from cell wall treated with polygalacturonase and mixed enzyme were higher than those of untreatment and $\beta$-galactosidase treatment.

• Asian-Australasian Journal of Animal Sciences
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• v.27 no.2
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• pp.290-301
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• 2014

The first purpose of this review is to outline some of the background information necessary to understand the mechanisms of action of fibre-degrading enzymes in non-ruminants. Secondly, the well-known and understood mechanisms are described, i) eliminating the nutrient encapsulating effect of the cell wall and ii) ameliorating viscosity problems associated with certain Non Starch Polysaccharides, particularly arabinoxylans and ${\beta}$-glucans. A third, indirect mechanism is then discussed: the activity of such enzymes in producing prebiotic oligosaccharides and promoting beneficial cecal fermentation. The literature contains a wealth of information on various non starch polysaccharide degrading enzyme (NSPase) preparations and this review aims to conclude by discussing this body of work, with reference to the above mechanisms. It is suggested that the way in which multi- versus single-component products are compared is often flawed and that some continuity should be employed in methods and terminology.

• Journal of Microbiology and Biotechnology
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• v.24 no.10
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• pp.1427-1437
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• 2014

Enzymatic hydrolysis of lignocellulosic biomass into fermentable sugars is a key step in the conversion of agricultural by-products to biofuels and value-added chemicals. Utilization of a robust microorganism for on-site production of biomass-degrading enzymes has gained increasing interest as an economical approach for supplying enzymes to biorefinery processes. In this study, production of multi-polysaccharide-degrading enzymes from Aspergillus aculeatus BCC199 by solid-state fermentation was improved through the statistical design approach. Among the operational parameters, yeast extract and soybean meal as well as the nonionic surfactant Tween 20 and initial pH were found as key parameters for maximizing production of cellulolytic and hemicellulolytic enzymes. Under the optimized condition, the production of FPase, endoglucanase, ${\beta}$-glucosidase, xylanase, and ${\beta}$-xylosidase was achieved at 23, 663, 88, 1,633, and 90 units/g of dry substrate, respectively. The multi-enzyme extract was highly efficient in the saccharification of alkaline-pretreated rice straw, corn cob, and corn stover. In comparison with commercial cellulase preparations, the BCC199 enzyme mixture was able to produce remarkable yields of glucose and xylose, as it contained higher relative activities of ${\beta}$-glucosidase and core hemicellulases (xylanase and ${\beta}$-xylosidase). These results suggested that the crude enzyme extract from A. aculeatus BCC199 possesses balanced cellulolytic and xylanolytic activities required for the efficient saccharification of lignocellulosic biomass feedstocks, and supplementation of external ${\beta}$-glucosidase or xylanase was dispensable. The work thus demonstrates the high potential of A. aculeatus BCC199 as a promising producer of lignocellulose-degrading enzymes for the biomass conversion industry.

• Asian-Australasian Journal of Animal Sciences
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• v.12 no.6
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• pp.988-1001
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• 1999

The rumen ecosystem is increasingly being recognized as a promising source of superior polysaccharide-degrading enzymes. They contain a wide array of novel enzymes at the levels of specific activities of 1,184, 1,069, 119, 390, 327 and $946{\mu}mol$ Reducing sugar release/min/mg protein for endoglucanase, xylanase, polygalactouronase, amylase, glucanase and arabinase, respectively. These enzymes are mainly located in the surface of rumen microbes. However, glycoside-degrading enzymes (e.g. glucosidase, fucosidase, xylosidase and arabinofuranosidase, etc.) are mainly located in the rumen fluid, when detected enzyme activities according to the ruminal compartments (e.g. enzymes in whole rumen contents, feed-associated enzymes, microbial cell-associated enzymes, and enzymes in the rumen fluid). Ruminal fungi are the primary contributors to high production of novel enzymes; the bacteria and protozoa also have important functions, but less central roles. The enzyme activities of bacteria, protozoa and fungi were detected 32.26, 19.21 and 47.60 mol glucose release/min/mL mediem for cellulose; 42.56, 14.96 and 64.93 mmol xylose release/min/mL medium after 48h incubation, respectively. The polysachharide-degrading enzyme activity of ruminal anaerobic fungi (e.g. Neocallimastix patriciarum and Piromyces communis, etc.) was much higher approximately 3~6 times than that of aerobic fungi (e.g. Tricoderma reesei, T. viridae and Aspergillus oryzae, etc.) used widely in industrial process. Therefore, the rumen ecosystem could be a growing source of novel enzymes having a tremendous potential for industrial applications.

• Korean Journal of Microbiology
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• v.54 no.3
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• pp.299-301
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• 2018

Microbulbifer agarilyticus GP101 was isolated from the gut of a marine invertebrate Turbo cornutus and capable of degrading polysaccharide such as agar, alginate, and ${\kappa}$-carrageenan constituting algal cell wall. To obtain genomic basis of polysaccharide-degrading activity, we sequenced genome of strain GP101. The genome consists of 4,255,625 bp, 3,458 coding sequences with 55.4% G + C contents. BLASTP search revealed the presence of seven agarases, five alginate lyases, ten glucanases, four chitinases, two xylanases, one ${\kappa}$-carrageenase, and one laminarinase. The genomic data of strain GP101 will provide potential uses in the bioconversion process of diverse polysaccharide into bioenergy and biochemicals.

• Microbiology and Biotechnology Letters
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• v.39 no.3
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• pp.189-199
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• 2011

Recently seaweed polysaccharides have been extensively studied due to their various biological functions including antitumor, antiviral, anticoagulant, and anti-inflammatory activities. Although seaweed polysaccharides are known to possess numerous beneficial properties, their industrial applications have been limited due to the low inclusion efficiency and high cost of manufacturing involved in chemical hydrolysis. In addition, the smell of seaweed has been a limiting factor in its application in the food and cosmetic industries. Therefore, novel hydrolysis methods and the deodorization of seaweed are required if the extensive application of seaweed polysaccharides is to be seen. A number of studies have examined various seaweed polysaccharide-degrading enzymes, which have been isolated from marine microorganisms, and enzymatic hydrolysis processes have been investigated for the improvement of production yields and the bioefficacy of seaweed polysaccharides. This review is a synopsis on the properties of seaweed polysaccharides-degrading enzymes from marine microorganisms and their industrial applications. The review reveals the pressing need for more concentrated research on the development of new biological materials from seaweed.

• Korean Journal of Microbiology
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• v.54 no.4
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• pp.463-464
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• 2018

Tamlana sp. UJ94 isolated from seawater can degrade alginate. To identify the genomic basis of this activity, the genome was sequenced. The genome was composed of 4,116,543 bp, 3,609 coding sequences, and 35.2 mol% G + C content. A BLASTp search predicted the presence of 9 alginate lyases as well as 6 agarases, 5 amylases, 4 carrageenases, 1 cellulase, 4 pectate lyases, and 7 xylanases, indicating its ability to degrade diverse polysaccharides. The genome of strain UJ94 is a source of polysaccharide-degrading enzymes for bioconversion processes.

• Journal of Microbiology and Biotechnology
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• v.19 no.6
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• pp.573-581
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• 2009

The complex enzyme pool secreted by the phytopathogenic fungus Fusarium graminearum in response to glucose or hop cell wall material as sole carbon sources was analyzed. The biochemical characterization of the enzymes present in the supernatant of fungal cultures in the glucose medium revealed only 5 different glycosyl hydrolase activities; by contrast, when analyzing cultures in the cell wall medium, 17 different activities were detected. This dramatic increase reflects the adaptation of the fungus by the synthesis of enzymes targeting all layers of the cell wall. When the enzymes secreted in the presence of plant cell wall were used to hydrolyze pretreated crude plant material, high levels of monosaccharides were measured with yields approaching 50% of total sugars released by an acid hydrolysis process. This report is the first biochemical characterization of numerous cellulases, hemicellulases, and pectinases secreted by F. graminearum and demonstrates the usefulness of the described protein cocktail for efficient enzymatic degradation of plant cell wall.

• Journal of Microbiology and Biotechnology
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• v.30 no.1
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• pp.79-84
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• 2020

This study investigated the characterization and functionality of Undaria pinnatifida root (UPT) extracts, degraded using a crude enzyme from Shewanella oneidensis PKA1008. To obtain the optimum degrading conditions, the UPT was mixed with alginate degrading enzymes from S. oneidensis PKA 1008 and was incubated at 30℃ for 0, 3, 6, 12, 24, and 48 h. The alginate degrading ability of these enzymes was then evaluated by measuring the reducing sugar, viscosity, pH and chromaticity. Enzymatic extract at 24 h revealed the highest alginate degrading ability and the lowest pH value. As the incubation time increased, the lightness (L ^⁎) also decreased and was measured at its lowest value, 39.84, at 12 hours. The redness and yellowness increased gradually to 10.27 at 6 h and to 63.95 at 3 h, respectively. Moreover, the alginate oligosaccharides exhibited significant anti-inflammatory activity. These results indicate that a crude enzyme from S. oneidensis PKA 1008 can be used to enhance the polysaccharide degradation of UPT and the alginate oligosaccharides may also enhance the anti-inflammatory effect.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.12
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• pp.1725-1731
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• 2002

The distribution and activities of hydrolytic enzymes (cellulolyti, hemicellulolytic,pectinolytic and others) in the rumen compartments of Hereford bulls fed 100% alfalfa hay based diets were evaluated. The alfalfa proportion in the diet was gradually increased for two weeks. Whole rumen contents were processed into four fractions: Rumen contents including both the liquid and solid fractions were homogenized and centrifuged, and the supernatant was assayed for enzymes located in whole rumen contents (WRE); rumen contents were centrifuged and the supernatant was assayed for enzymes located in rumen fluids (RFE); feed particles in rumen contents were separated manually, washed with buffer, resuspended in an equal volume of buffer, homogenized and centrifuged and supernatant was assayed for enzymes associated with feed particles (FAE); and rumen microbial cell fraction was separated by centrifugation, suspended in an equal volume of buffer, sonicated and centrifuged, and the supernatant was assayed for enzymes bound with microbial cells (CBE). It was found that polysaccharide-degrading proteins such as $\beta$-1,4-D-endoglucanase, $\beta$-1,4-D-exoglucanase, xylanase and pectinase enzymes were located mainly with the cell bound (CBE) fraction. However, $\beta$-D-glucosidase, $\beta$-D-fucosidase, acetylesterase, and $\alpha$-L-arabinofuranosidase were located in the rumen fluids (RFE) fraction. Protease activity distributions were 37.7, 22.1 and 40.2%, and amylase activity distributions were 51.6, 18.2 and 30.2% for the RFE, FAE and CBE fractions, respectively. These results indicated that protease is located mainly in rumen fluid and with microbial cells, whereas amylase was located mainly in the rumen fluid.