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송곳니구름버섯(Irpex zonatus) BN2에 의한 다핵방향족 탄화수소화합물의 분해
최양순,윤경하 순천향대학교 기초과학연구소 1996 순천향자연과학연구 논문집 Vol.2 No.2
우리 나라 자연 환경에서 분리 동정된 송곳니구름버섯 (Irpex zonatus) BN2 균주의 리그닌 분해효소활성과 anthracene, phenanthrene 및 benzo(a)pyrene의 분해능을 조사하였다. 송곳니구름버섯 BN2 균주는 lignin peroxidase (LiP) 와 veratryl alcohol oxidase (VAO)를 생산하지 않고 laccase와 manganese dependent peroxidase (MnP)를 생산했다. MnP는 배양 3일부터 생산되었으나 효소활성은 매우 낮았다. 반면 laccase는 배양 초부터 지속적으로 생산되었고 활성은 대단히 높았다. 균주를 PAHs 화합물에 접종하여 배양했을 때 anthracene 분해율은 배양 1주에서 74.6%, 2주에서 92.9%, 4주에서 100%의 분해율을 접종하여 나타났다. phenanthrene 의 경우 배양 1주와 2주에서 각각 74.3%와 91.6%의 분해율을 나타냈고 4주에서 100%의 분해율을 나타냈다. benzo(a)pyrene 은 각각 41.8%, 49.0% 및 82.5%의 분해율을 나타내서 다른 PAHs 화합물보다 비교적 낮은 분해율을 보였다. 본 실험 결과 송곳니구름버섯 BN2 균주에 의한 PAHs 화합물의 분해는 주로 laccase에 의하여 이루어진다고 생각된다. The present research was undertaken to investigate the activity of ligninolytic enzymes and the biodegradation capability of polycyclic aromatic hydrocarbons (PAHs) with Irpex zonatus BN2, isolated from nature and identified. For the assay of enzyme activities, the isolate did not produce lignin peroxidase (LiP) and veratryl alcohol oxidase (VAO), but laccase and manganese dependent peroxidase (MnP). While the activity for MnP was low (61.6 n㏖/㎎·protein). its laccase activity was very high (1185.9 n㏖/㎎·protein). Moreover. laccase had appeared earlier than MnP When the isolate was incubated with 10㎎/L (final concentration) of anthracene, phenanthrene and benzo(a)pyrene, the isolate removed anthracene 74.6%, 92.9%, and 100% respectively for 7,14 and 28 days incubation. In case of phenanthrene was 74.3%, 91.6% and 100% respectively. Finally the results of benzo(a)pyrene was 41.8%, 49.0% and 82.5%, respectively. The results suggest that laccase of Irpex zonatus BN2 should play an important role in the biodegradation of these PAHs compounds.
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삼색도장벗(Daedaleopsis tricolor)P3에 의한 염료의탈색
윤경하,최양순 순천향대학교 기초과학연구소 1997 순천향자연과학연구 논문집 Vol.3 No.2
The present research was undertaken to investigate the activity of ligninolytic enzymes and the decolorization capability of some dyes with Daedaleopsis tricolor P3, isolated from nature and identified. For the assay of enzyme activities, the isolate produced lignin peroxidase(LiP), veratryl alcohol oxidase(VAO), laccase and manganese dependent peroxidase(MnP). At first, laccase and VAO were secreted as early as on day 2, but laccase activity was higher than VAO, and increased gradually, peaking on day 6 (89.1nmol/mg·protein). While LiP appeared on day 5 later than MnP, and increased significantly peaking on day 7 (50.4nmol/mg·protein). When the isolate was incubated with each dye for 10 days, the decolorization rates of azo dyes, such as orange Ⅱ, orange G, tropaeolin O and congo red were 90.7%, 89.7%, 88.4% and 82.4%, respectively. In case of heterocyclic dyes, eosin Y, toludine blue, methyl blue and azur B were 97.7%, 96.4%, 98.3% and 92.7% respectively. Finally those of triphenylmethane dye such as basic fuchsin, malachite green and crystal violet were 98.2%, 93.6% and 99.0%, respectively. This results suggest that laccase and VAO of Daedaleopsis tricolor P3 should be played an important role in the decolorization of the dyes.
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구름버섯(Coriolus versicolor) VK7 에 의한 Anthracene, Phenanthrene 및 Benzo(α)pyrene 의 분해
윤경하,최양순 순천향대학교 기초과학연구소 2001 순천향자연과학연구 논문집 Vol.7 No.1
The present research was undertaken to investigate the activity of ligninolytic enzymes and the biodegradation capability of anthracene, phenanthrene and benzo(α)pyrene with Coriolus versicolor VK7, isolated from nature and identified. For the assay of enzyme activities, the isolate did not produce lignin peroxidase (LiP) and veratryl alcohol oxidase (VAO), but laccase and manganese dependent peroxidase (MnP). While the activity for MnP was low (22.2 nmol/mgㆍprotein), its laccase activity was very high (740.0 nmol/mgㆍprotein). Moreover, laccase had appealed earlier than MnP. When the isolate was incubated with 10mg/L (final concentration) of anthracene, phenanthrene and benzo(α)pyrene, the isolate removed anthracene 74.1%, 86.1% and 100%, respectively for 7, 14 and 28 days incubation. In case of phenanthrene was 70.3%, 89.2% and 100%, respectively. Finally the results of benzo(α)pyrene was 58.3%, 64.8% and 84.8%, respectively. The resells suggest that laccase of Coriolus versicolor VK7 should play an important role in the biodegradation of these PAHs compounds.
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