• Mycobiology
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• v.33 no.4
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• pp.188-193
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• 2005

Twenty nine samples of pigeon droppings (n = 12) and soil contaminated with avian excreta (n = 19), collected from different sites in Busan, were examined for isolation and characterization of Cryptococcus neoformans. Of these samples, 5 strains of C. neoformans were recovered from pigeon droppings (5/12 : 41.7%). All isolates were belonged to C. neoformans var. grubii (serotype A). The extracellular enzyme activities of the strains by using the API-ZYM system showed two different enzymatic patterns. The genetic variability among C. neoformans isolates was analyzed by random amplified polymorphic DNA (RAPD) using three 10-mer primers. Two different RAPD patterns, which clearly distinguished the isolates, were identified. Analysis of RAPD patterns provided a good characterization of environmental strains of C. neoformans serotype A as a heterogeneous group and were in good agreement with enzymatic profiles.

• Korean Journal of Plant Resources
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• v.21 no.3
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• pp.222-225
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• 2008

Chemical composition and enzymatic saccharification characteristics of hemp woody core were investigated by their chemical composition analysis and enzymatic saccharification with commercially available cellulases (Celluclast 1.5L and Novozym 342). Hemp woody core have higher xylan and lower lignin contents than its bast fiber. Based on hemicelluloses and lignin composition, hemp woody core is similar with hardwood biomass. However, cellulose was more easily converted to glucose than xylan to xylose and this trend was confirmed both hemp woody core and yellow poplar. Hemp woody core biomass shows higher saccharification than yellow poplar (hardwood biomass) based on cellulose and xylan hydrolysis. With easier enzymatic saccharification in cellulose and xylan, and similar chemical composition, hemp woody core have better biorefinery feedstock characteristics than hardwood biomass.

• YAKHAK HOEJI
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• v.49 no.3
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• pp.198-204
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• 2005

Human foamy virus (HFV) integrase mediates integration of viral c-DNA into cellular DNA. In this process, HFV integrase recognizes its own viral DNA specifically and catalyzes insertion of viral c-DNA. In order to study catalytic domains and residues, three deletion mutants and two point mutants of HFV integrase were constructed and analyzed with respect to enzymatic activities. The C-terminal deletion mutant showed decreased enzymatic activities while the N-terminal deletion mutant lost the activities completely, indicating that the N-terminal domain is more important than the C-terminal domain in enzymatic reaction. The point mutants, in which an aspartic acid at the 164th position or a glutamic acid at the 200th position of the HFV integrase protein was changed to an alanine, lost the enzymatic activities completely. However, they were well complemented with other defective deletion mutants to recover enzymatic activities partially. Therefore, these results suggest that the aspartic acid and glutamic acid at the respective 164th and 200th positions are catalytic residues for enzymatic reaction.

• Journal of the Korean Wood Science and Technology
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• v.50 no.6
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• pp.436-447
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• 2022

Lignocellulose nanofibrils (LCNFs) were prepared using a two-step deep eutectic solvent (DES) and enzymatic pretreatment followed by mechanical defibrillation, and we examined the effects of enzymatic pretreatment conditions on different characteristics of the LCNFs thus obtained. The LCNFs yielded using the two-step DES pretreatment (Enz-LCNF) exhibited a well-defibrillated entangled web-like structure with an average fiber diameter ranging from 15.7 to 20.4 nm. Furthermore, we found that the average diameter and filtration time of the Enz-LCNFs decreased with an increase in enzyme concentration and enzymatic treatment time, whereas we detected a concomitant reduction in the tensile strength of the Enz-LCNF sheets. The Enz-LCNFs were characterized by a typical cellulose I structure, thereby indicating that the enzymatic treatment causes very little damage to the crystalline form.

• Journal of Microbiology and Biotechnology
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• v.20 no.12
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• pp.1711-1716
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• 2010

A gene encoding the ${\beta}$-xylosidase/${\alpha}$-arabinofuranosidase (XylC) of Paenibacillus woosongensis was cloned into Escherichia coli. This xylC gene consisted of 1,425 nucleotides, encoding a polypeptide of 474 amino acid residues. The deduced amino acid sequence exhibited an 80% similarity with those of both Clostridium stercorarium ${\beta}$-xylosidase/${\alpha}$-N-arabinosidase and Bacillus cellulosilyticus ${\alpha}$-arabinofuranosidase, belonging to the glycosyl hydrolase family 43. The structural gene was subcloned with a C-terminal His-tag into a pET23a(+) expression vector. The His-tagged XylC, purified from a cell-free extract of a recombinant E. coli BL21(DE3) Codon Plus carrying a xylC gene by affinity chromatography, was active on para-nitrophenyl-${\alpha}$-arabinofuranoside (pNPA) as well as para-nitrophenyl-${\beta}$-xylopyranoside (pNPX). However, the enzymatic activities for the substrates were somewhat incongruously influenced by reaction pHs and temperatures. The enzyme was also affected by various chemicals at different levels. SDS (5 mM) inhibited the enzymatic activity for pNPX, while enhancing the enzymatic activity for pNPA. Enzyme activity was also found to be inhibited by addition of pentose or hexose. The Michaelis constant and maximum velocity of the purified enzyme were determined for hydrolysis of pNPX and pNPA, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.6
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• pp.1143-1147
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• 1998

Enzymatic characterization of peroxidase(E.C. 1.11.1.7) from soybean sprouts was investigated. The optimum pH of the purified peroxidase was 7.0 and relatively stable at pH 6.0~7.0. And the optimum temperature was 50oC. The enzyme was most active with guaiacol as a substrate, followed by (＋)catechin, pyrogallol and p phenylenediamine. The Km values for guaiacol and H2O2 were 4.2mM and 2.5mM, respectively. L Ascorbic acid and 2 mercaptoethanol greatly inhibited the enzyme activity, while Cu2+, Co2+ and Ni2+ activated the enzyme.

• Journal of Microbiology and Biotechnology
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• v.13 no.1
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• pp.35-42
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• 2003

A 1,3 kb cellulase gene encoding novel bifunctional cellulase-chitosanase activity was cloned from biopolymer-producing alkali-tolerant B. lichenformis NBL420 in E. coli. A recombinant cellulase-chitosanase, named CelA, was expressed and purified to homogeneity. The activity staining and the enzymatic characterization of the purified CeIA revealed bifunctional activities on carboxymethyl cellulose (CMC) and glycol-chitosan. The similar characteristics of the enzymatic activities at the optimum pH, optimum temperature, and thermostability Indicated that CelA used a common catalytic domain with relaxed substrate specificity. A comparison of the deduced amino acids in the N-terminal region revealed that the mature CelA had a high homology with the previously identified bifunctional cellulase-chitosanase of Myxobacter sp. AL- 1.

• 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.

• Korean Journal of Veterinary Research
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• v.34 no.4
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• pp.781-785
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• 1994

Uridine diphosphate(UDP)-galactose-4-epimerase-less mutants of Salmonella pullorum were isolated after mutagenic treatment with ethidium bromide. When isolated gal E mutants of S. pullorum A2 and D1 were grown in the presence of galactose(0.1 W/V), they exhibited marked bacteriolysis in heart infusion broth. The mutant strains were further investigated the characteristics of enzymatic activities in the Leoloir galactose pathway. Isolated A2 and D1 strains were completely deficient in UDP-galactose-4-epimerase activity. And the activity of other enzymes involved in galactose metabolism were reduced significantly.

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.496-496
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• 2003