느티만가닥버섯의 신품종에 대한 endo-, exo-cellular 효소 활성도의 비교

국문 초록 (Abstract)

본 연구는 새롭게 개발된 느티만가닥버섯의 6개 품종에 대한 형태적, 생리적 특성을 조사하고 endo-, exo-cellular 효소 활성을 측정하기 위해서 수행되었다. 국내 야생종인 Hm3-10과 일본 재배종인 Hm1-1과의 단핵균사 교배를 통하여 343개의 교배 균주를 획득하여 재배를 실시하여 58개 균주를 1차 선발하고 2차로 6개 균주를 선발하였다. 6개 선발 균주를 대상으로 배양 일수 별로 재배를 실시한 결과 배양일수가 80일 이상에서는 재배일수가 19~20일로 단축되어 최적 배양일수를 80일로 결정하였다. 80일 배양일수에서 각 품종별 형태적 특성을 검증한 결과 Hm15-3, Hm15-4, Hm17-5의 3균주가 재배에 적합한 균주로 판명되었다. 각 균주의 endo-cellular 효소 활성도를 측정한 결과, α-amylase의 효소 활성도가 73.9~102,2 unit/㎎ protein으로 가장 높았으며, chitinase 의 효소활성도가 8.1~13.1 unit/㎎ protein으로 측정되었다. Exo-cellular효소 활성도를 측정한 결과, α-amylase의 효소활성도가 5,292~1,184 unit/㎎ protein으로 가장 높았으며, CMCase와 Xylanase의 효소 활성도가 각각 1,140~245 unit/㎎ protein, 94~575 unit/㎎ protein으로 측정되었다. 그러나 β-glucosidase와 chitinase의 활성도는 비교적 낮은 활성도를 나타내었다.

다국어 초록 (Multilingual Abstract)

This study was carried out to investigate the morphological and physiological characteristics of six new cultivars of Hypsizygus marmoreus (Hm) and measure endo-, exo-cellular enzyme-specific activity. The domestic wild stain (Hm3-10) and commercial strain in Japan (Hm1-1) were mated by crossing monokaryon mycelia. We gained 58 strains from one of 400 crosses through the 1<SUP>st</SUP> cultivation experiment, and selected six strains from one of 58 strains through the 2<SUP>nd</SUP> cultivation experiment. When six of the selected new strains were grown during several spawn culture periods (60, 70, 80, 90, and 100 days), a spawn culture period of more 80 days was considered to be excellent as being shorter than 19~20 days. Therefore, we determined the period of spawn culture as 80 days. Three strains such as Hm15-3, Hm15-4, and Hm17-5 showed an excellent result. When endo-cellular enzyme activity measured eight strains, we obtained a result of that specific activity of α-amylase at the highest as 73.9~102.2 unit/㎎ protein, and chitinase is lower than α-amylase at 8.1~13.1 unit/㎎ protein. When exo-cellular enzyme activity measured eight strains, we determined the result of that specific activity of α-amylase is the highest at 5,292~1,184 unit/㎎ protein, and CMCase and xylanase were 1,140~245 unit/㎎ protein, 94~575 unit/㎎ protein, compared to each other. However, the enzyme activity of β-glucosidase and chitinase is low.

목차 (Table of Contents)

• 서론
• 재료 및 방법
• 결과 및 고찰
• 감사의 글
• References
• 초록

참고문헌 (Reference)

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