• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.1
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• pp.47-53
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• 2010

Bacteria strains with high activities of extracellular enzymes (protease, fibrinolytic enzyme, amylase, cellulase, and lipase) were isolated from Jeju traditional fermented soybean paste (Doenjang), and characterized by 16S rRNA gene sequence analysis and physiological properties. Protease activities were higher in JR14, JR19, JR25, JR32, JR38, JR47, and JR64 than Bacillus subtilis KCCM 12027 (standard strain). Amylase activities were shown in JR6, JR25, JR38, JR56 and JR81, while not in KCCM12027. Cellulase activities were higher in JR6, JR14, JR48, and JR65 than those of other isolated strains and KCCM 12027 whereas lipase activities were the higher in JR-14 and JR-48. Thrombolytic activity in JR19 with high hemolysis activity were 192% compared with that of plasmin as a positive control. Zymogram analysis indicated that the thrombolytic active strains had 4~5 bands in the molecular weight range of 25~75 kDa. Gene sequence analysis of rRNA revealed that the isolated stains had 99% homology with Bacillus species, and the thrombolytic active stain JR19 was B. stratosphericus $41KF2a^T$.

• Journal of Life Science
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• v.19 no.11
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• pp.1617-1622
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• 2009

Optium conditions for the production of mycelia and extracellular polysaccharide (EXPS) from submerged mycelial culture of Inonotus obliquus and their immunomodulating activities were investigated. The optmium production of mycelia and EXPS from I. obliquus was observed in mushroom complete medium (MCM). The optimum pH, temperature, and agitation speed for the production of mycelia and EXPS were 5.5, $25^{\circ}C$, and 150 rpm, respectively. The culture period for maximum production of mycelia (10.89 g/l) and EXPS (1.25 g/l) in shake flask cultivation was 11 days. The anticomplementary activity of intracellular polysaccharide (INPS) and EXPS form I. obliquus increased in a dose-dependent manner. Lysosomal enzyme activity of EXPS and INPS increased by 2.0- and 2.2-fold at $100{\mu}g/ml$ concentration, respectively, compared to the control group.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.36 no.3
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• pp.9-14
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• 2004

The useful fungi which secret extracellular enzymes was selected for deinking agent of old newsprint. Five fungal strains were isolated from a paper mill soil ground. The CMCase, FPase and xylanase activities of fungi on the liquid culture were investigated at optimal growth conditions. The results of this study were as follow: The optimal pH and temperature for culture growth were 4～8 and 27～$35^{\circ}C$, respectively. For screening of extracellular enzymes at optimal culture conditions the optimal culture period were less than 6-7 days. Fusarium pallidoroseum and Aspergiilus niger which shows relatively higher CMCase, FPase and xylanase activities than the other species were selected for further enzymatic deinking research.

• Microbiology and Biotechnology Letters
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• v.25 no.2
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• pp.115-120
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• 1997

Penicillium sp.-L4, a causative fungus of rot in citrus fruits, was isolated and its mode of hydrolytic enzyme production was investigated. Carboxymethylcellulase (CMCase), polygalacturonase(PGase), extra- & intra-cellular $\beta$-glucosidase and cellobiase were produced drastically by addition of substrates in minimal media. Production of the hydrolytic enzymes were induced efficiently by cellobiose and cellooligosaccharides which were the products of cellulose hydrolysis, but repressed by addition of mono-saccharide such as glucose, raffinose, galacturonic acid. The relative activity of p-nitrophenyl-$\beta$-D-glucopyranoside(PNPG) hydrolysis was higher than that of cellobiose hydrolysis in extracellular enzymes, and reverse is true in intracellular enzymes. Intact enzyme production of P. sp.-L4 on lemon peel lesion was sequential. $\beta$-Glucosidase and CMCase were produced first and followed by PGase. The enzyme productivities and pH in lesions were coincident with optimal pH of each enzyme activities.

• Journal of the Korean Wood Science and Technology
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• v.41 no.1
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• pp.19-32
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• 2013

In this study, outstanding white rot fungi for biodegradation of organosolv lignin were selected on the basis of their ligninolytic enzyme system. Fifteen white rot fungi were evaluated for their ability to decolorize Remazol Brilliant Blue R (RBBR) in SSC and MEB medium, respectively. Six white rot fungi (Ceriporiopsis subvermispora, Ceriporia lacerate, Fomitopsis insularis, Phanerochaete chrysosporium, Polyporus brumalis, and Stereum hirsutum) decolorized RBBR rapidly in SSC medium within 3 days. The protein contents as well as the activities of manganese peroxidase (MnP) and laccase for 6 selected fungi were determined on the SSC medium with and without organosolv lignin. Interestingly, extracellular protein concentrations were determined to relative higher for S. hirsutum and P. chrysosporium in the presence of organosolv lignin than others. On the other hands, each fungus showed a different ligninolytic enzyme pattern. Among them, F. insularis resulted the highest ligninolytic enzyme activities on incubation day 6, indicating of 1,545 U/mg of MnP activity and 1,259 U/mg of laccase activity. In conclusion, $STH^*$ and FOI were considered as outstanding fungi for biodegradation of organosolv lignin, because $STH^*$ showed high extracellular protein contents and ligninolytic enzyme activities over all, and ligninolytic enzyme activities of FOI were the highest among white rot fungi used in this study.

• Journal of Microbiology and Biotechnology
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• v.16 no.10
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• pp.1613-1621
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• 2006

Isolation and identification of algal lytic bacteria were carried out. Nine strains of algal lytic bacteria were isolated by the double-layer method using Anabaena flos-aquae as a sole nutrient. The isolate, AFK-13, showing the highest algal lytic activity was identified as Sinorhizobium kostiense based on the l6S rDNA sequence. The algal lytic experiments of the culture supernatants of AFK-13 demonstrated that the bacterial cell growth reached a maximum at 36-h culture, but the supernatant of 72-h culture exhibited the highest activity. Components among the extracellular products in the crude enzyme of the supernatant from S. kostiense AFK-13 culture were responsible for degradation of cell walls of Anabaena flos-aquae. Algal lytic assay tests of the culture supernatants suggest that the main substances for algal lytic activity could be proteinaceous. The activity of glucosidase was observed highly by polysaccharolytic analysis using the crude enzyme from S. kostiense AFK-13, whereas activities of galactosidase, mannosidase, rhamnosidase, and arabinosidase were also detected in low levels. The molecular weights (MW) of ${\alpha}-\;and\;{\beta}$-glucosidases were estimated to be approximately 50-100 kDa by the ultrafiltration method.

• Mycobiology
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• v.39 no.2
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• pp.118-120
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• 2011

The ability of Ganoderma to produce extracellular enzymes, including ${\beta}$-glucosidase, cellulase, avicelase, pectinase, xylanase, protease, amylase, and ligninase was tested in chromogenic media. ${\beta}$-glucosidase showed the highest activity, among the eight tested enzymes. In particular, Ganoderma neo-japonicum showed significantly stronger activity for ${\beta}$-glucosidase than that of the other enzymes. Two Ganoderma lucidum isolates showed moderate activity for avicelase; however, Ganoderma neojaponicum showed the strongest activity. Moderate ligninase activity was only observed in Ganoderma neo-japonicum. In contrast, pectinase, amylase, protease, and cellulase were not present in Ganoderma. The results show that the degree of activity of the tested enzymes varied depending on the Ganoderma species tested.

• Mycobiology
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• v.35 no.3
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• pp.162-165
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• 2007

Thirty seven species of Fusarium were evaluated for their ability of producing extracellular enzymes using chromogenic medium containing substrates such as starch, cellobiose, CM-cellulose, xylan, and pectin. Among the tested species Fusarium mesoamericanum, F. graminearum, F. asiaticum, and F. acuminatum showed high ${\beta}$-glucosidase acitivity. Xylanase activity was strongly detected in F. proliferatum and F. oxysporum. Strong pectinase activity was also found in F. oxysporum and F. proliferatum. Amylase activity was apparent in F. oxysporum. No clear activity in cellulase was found from all the Fusarium species tested.

• Korean Journal of Ecology and Environment
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• v.39 no.4 s.118
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• pp.435-444
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• 2006

A suite of extracellular enzyme activities involved in organic carbon decomposition were determined in three northern peatlands (a bog, a fen, and a swamp) over a 12 month period along with trace gas ($CO_2$ and $N_2O$) flux and DOC dynamics in the wetlands. The activities varied $0.008-0.066\;{\mu}mole\;g^{-1}\;min^{-1}$, $0.003-0.021\;{\mu}mole\;g^{-1}\;min^{-1}$, $0.003-0.016\;{\mu}mole\;g^{-1}\;min^{-1}$, $0.004-0.047\;{\mu}mole\;g^{-1}\;min^{-1}$, for ${\beta}-glucosidase$, cellobiohydrolase, ${\beta}-xylosidase$, and N-acetylglucosaminidase, respectively. In general, the activities were highest in the forested swamp followed by the fen and the bog. When the data from three wetlands are combined, the enzyme activities exhibited significant positive correlations with trace gas emission and available carbon. Further, the average activity of 4 enzymes explained about 20-40% of the variations of trace gas emssion and available carbon. The results indicate that enzymes related to the mineralization of organic carbon may play an important role in trace gas flux and DOC dynamics in northern peatlands.

• Journal of Microbiology and Biotechnology
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• v.17 no.5
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• pp.761-768
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• 2007

Serratia proteamaculans HY-3 isolated from the digestive tract of a spider produces an extracellular protease named arazyme, with an estimated molecular mass of 51.5 kDa. The purified enzyme was characterized as having high activities at wide pH and temperature ranges. We further characterized biochemical features of the enzymatic reactions under various reaction conditions. The protease efficiently hydrolyzed a broad range of protein substrates including albumin, keratin, and collagen. The dependence of enzymatic activities on the presence of metal ions such as calcium and zinc indicated that the enzyme is a metalloprotease, together with the previous observation that the proteolytic activity of the enzyme was not inhibited by aspartate, cysteine, or serine protease inhibitors, but strongly inhibited by 1,10-phenanthroline and EDTA. The araA gene encoding the exoprotease was isolated as a 5.6 kb BamHI fragment after PCR amplification using degenerate primers and subsequent Southern hybridization. The nucleotide sequence revealed that the deduced amino acid sequences shared extensive similarity with those of the serralysin family of metalloproteases from other enteric bacteria. A gene(inh) encoding a putative protease inhibitor was also identified immediately adjacent to the araA structural gene.