• The Korean Journal of Mycology
• /
• v.27 no.4 s.91
• /
• pp.299-303
• /
• 1999

Phytase(myo-inositol-hexakis phosphate 3-phosphohydrolase, E C 3.1.3.8) sequentially hydrolyzes phytate to myo-inositol and inorganic phosphate. Phytase of Aspergillus ficuum was purified to homogeneity using ultrafiltration, cation exchange column and anion exchange column. It's molecular weight is estimated as around 90,000 by SDS-PAGE. Antibody against the phytase was produced by immunizing mice with the purified phytase. The titer of the antibody was determined to be 1/25,000.

• Microbiology and Biotechnology Letters
• /
• v.19 no.3
• /
• pp.253-258
• /
• 1991

- An exoinulinase (EC 3.2.1.80) was purified from a commercial inulinase preparation from Aspergillus ficuum using ion exchange chromatography on CM-Sephadex C-50 and DEAESepharose 6B and HPLC gel filtration on a Protein Pak 125 column. Native exoinulinase had a molecular weight of 83, 000$\pm$ 1, 000 and was glycoprotein. Optimal pHs of the enzyme were ranged from 4.4 to 4.7. About ninety five percent of the whole activity was maintained even after incubation of 8 hours at $55^{\circ}C$.The enzyme was a typical non-specific P-fructofuranosidase, of which I/S ratio appears to be 0.35.

• Mycobiology
• /
• v.28 no.3
• /
• pp.119-122
• /
• 2000

Phytases (myo-inositol hexakisphosphate phosphohydrolase; EC 3.1.3.8) are enzymes which catalyze the hydrolisys of phytate into myo-inositol and inorganic phosphates. Phytases are found in plants and a variety of microorganisms. Aspergillus species were treated with 254 nm of UV irradiation for the screening of phytase overproducing mutant strains. At 15 minute irradiation, the survivals of population were less than 5%, and UV irradiation time was decided at 20 minute for the isolation of mutant strains. Four UV mutant strains in A. oryzae (YUV-47, -169, -341, -511) and six in A. ficuum (FUV-17, -36, -69, -193, -317, -419) were isolated on PSM media containing ammonium phosphate. The specific enzyme activities of A. ficuum mutants are 110 to 140% higher than that of wild type.

• Microbiology and Biotechnology Letters
• /
• v.19 no.2
• /
• pp.158-162
• /
• 1991

Endoinulinase was purified from a commercial inulin preparation produced by Aspergillus ficuum using ion exchange chromatography on CM-Sephadex C-50 and DEAE-Sepharose 6B, HPLC gel filtration on a Protein Pak 125 Colum and HPLC ion exchange chromatography on a TSK DEAE-5pw Column. The endoinulinase had a molecular weight of 72,000${\pm}$1,000 and was glycoprotein with 23 to 25% w/w sugar content. The enzyme was much more active on inulin with random cleavage mode than on sucrose and on palatinose: The ration of activity on inulin and sucrose (I/S ratio) was 10~14.

• Microbiology and Biotechnology Letters
• /
• v.30 no.4
• /
• pp.305-311
• /
• 2002

Acetyl xylan esterase gene (AXE) from Aspergillus ficuum was cloned and its Pichia expression plasmid, pPICZ$\alpha$C-AXE (4.6 kb), was constructed, in which the AXE gene was under the control of the AOXI promoter and connected downstream of mating factor u-1 signal sequence. The plasmid linearized by Sacl was integrated into the 5'AOXI region of the chromosomal DNA of P. pastoris. In the flask batch culture of P. pastoris transformant on methanol medium, the cell concentration and total AXEase activity reached at 6.0 g-dry cell weight/1 and 77 unit/ml after 36 h cultivation, respectively. In the fed-batch culture employing the optimized methanol and histidine feeding strategy, the cell concentration and total AXEase activity were significantly increased to about 97 g-dry cell weight/1 and 930 unit/ml. Most of AXEase activity (>90%) was found in the extracellular medium and the majority of extracellular protein (>80%) was AXEase enzyme (33.5 kDa). This result means that about 9.8 g/1 of AXEase protein was produced in the extracellular medium.

• Journal of Veterinary Clinics
• /
• v.18 no.1
• /
• pp.18-21
• /
• 2001

In this study, we assessed the efficacy of a novel B. amyloliquefacience DS11 phytase (DS11 phytase) and that of a commercial Aspergillus ficcum phytase (AF phytase) through their bioavailabilities of phytin-posphorus and -calcium in the diet using cannulated pigs. For the purpose of evaluating the efficacy of the phytases in pigs, we determined phosphorous concentrations from serum and feces, in addition to ingesta obtained from the cannula at the terminal ileum. As results, phosphorus concentration was lower in feces from DS11 group and BASF group by 17% and 10%, and higher in serum from the respective groups by 34% and 20%, as compared to the control group. Both phytases are evaluated to enhance phosphorus availability to the great extent. Calcium concentration of feces were lower in DS11 group and BASF group by 31% and 10%, than that in the control. Calcium concentration of serum was higher in DS11 phytase group by 4% but lower in AF phyase group by 3%, then that in the control group.

• Microbiology and Biotechnology Letters
• /
• v.8 no.1
• /
• pp.47-53
• /
• 1980

For the Purpose of studies on the citric acid fermentation, 579 strains of Aspergilli were isolated from natural sources of microorganisms. Out of them, the strains of M-80 and M-315 which produced relatively larger amount of citric acid than any others were selected after calling out an extensive screening test. The results obtained in light of the manual of Raper had been shown that the selected strains of M-80 and M-315 were identified as Aspergillus usamii mut. shirousamii, Aspergillus ficuum, respectively.

• 한국생물공학회:학술대회논문집
• /
• 2000.04a
• /
• pp.153-156
• /
• 2000

Xylan, the major hemicellulose component of many plants, occurs naturally in a partially acetylated form and lignin, the most resistant component in plant cell wall degradation, is also attached to ${\beta}-1,4-linked-D-xylose$ backbone through the ester linkage. Esterases are required to release the esterified substituent and acetyl esterases are important in the complete degradation of acetylated polysaccharides, like pectins and xylans. The gene(Axe) encoding acetyl xylan estarase(AXE) was isolated from genomic ${\lambda}$ library from Aspergillus ficuum. Nucleotide sequencing of the Axe gene indicated that the gene was separated with two intervening sequences and the amino acid sequence comparison revealed that it was closely related to that from A. awamori with the 92 % indentity. Heterologous expression of AXE was conducted by using YEp352 and Saccharomyces cerevisae 2805 as a vector and host expression system, respectively. The Axe gene was placed between GAL1 promoter and GAL7 terminator and then this recombinant vector was used to transform S. cerevisiae 2805 strain. Culture filtrate of the transformed yeast was assayed for the presence of AXE activity by spectrophotometry and, comparing with the host strain, four to five times of enzyme activity was detected in culture filtrate of transformed yeast.

• Asian-Australasian Journal of Animal Sciences
• /
• v.13 no.5
• /
• pp.673-680
• /
• 2000

An experiment was conducted with day-old 300 commercial male broiler chicks (Arbor Acres$^{(R)}$) to evaluate the efficacy of crude phytase preparerations produced from a culture of Aspergillus ficcum. The experiment consisted of five dietary treatments; T1, com-soy control diet with 0.45% non-phytate phosphorus (NPP) for starter period and 0.35% NPP for grower period; T2, control - 0.1% NPP; T3, control 0.2% NPP; T4, T3+600 U of crude phytase (broth+cell); and T5, T3+600 U of crude phytase (broth). The body weight gain, feed intake, and feed/gain of chickens fed T1 diet was highest (p<0.01) among treatments. BW gain and feed intake of T4 and T5 were greater than those of T3 but were less than those of T1 and T2. T3 was highest in mortality among treatments. Decreasing the NPP level lowered availability of DM, crude ash, ether extract, crude fiber, Zn, and Fe but supplementation of crude phytase preparations improved the availability of these nutrients as well as those of Ca, P and Cu. Excretion of P and Cu significantly decreased as the NPP level in the diet decreased. Further reduction of P and Cu excretion and reduction of Ca, Mg and Fe excretion were achieved by supplementation of crude phytase preparations. The serum concentrations of Ca, P, Mg, Zn, Fe, and Cu were significantly increased by crude phytase supplementation. The weight and length of tibia, and contents of crude ash, Ca, P, Mg, and Zn were adversely affected by lowering NPP level but partially recovered by supplementation of crude phytase preparations. In conclusion, lowering NPP level in the broiler diet significantly depressed the performance. Supplementation of crude phytase preparations produced from Aspergillus ficuum could partially recover the depression.

• KSBB Journal
• /
• v.13 no.3
• /
• pp.284-288
• /
• 1998

Production of inulo-oligosaccharides from inulin was carried out with the maximum yield of 94% using a purified endoinulinase from Aspergillus ficcum. The optimum reaction temperature and pH were 55-60$^{\circ}C$ and pH 5.5-6.0, respectively. The Michaelis constant and maximum reaction velocity of the endoinuinase for inulin were 13.27 g/L and 0.13 g/L$.$min at 55$^{\circ}C$, pH 5.5, respectively. Inulin source had no significant effect on oligosaccharide yield and product composition, although initial production rate differed according to inulin origins. The reaction pH was a critical factor in inulo-oligosaccharide production because considerable free monosaccharides were released, decreasing oligosaccharide yield at low pH conditions. An empirical relationship describing the reaction performance was developed from kinetic data: the time to reach maximum oligosaccharide yield (tw) as a function of initial concentration of inulin (lo) and enzyme (Eo); i.e., log tM = -1.025 log Eo - 0.011 l0 + 2.655.