华北农学报
華北農學報
화북농학보
ACTA AGRICULTURAE BOREALI-SINICA
2015年
2期
124-127
,共4页
田兆丰%刘霆%吴慧玲%厚凌宇%刘伟成
田兆豐%劉霆%吳慧玲%厚凌宇%劉偉成
전조봉%류정%오혜령%후릉우%류위성
小链霉菌%抗病毒组分%分离纯化%稳定性
小鏈黴菌%抗病毒組分%分離純化%穩定性
소련매균%항병독조분%분리순화%은정성
Streptonyces parvus%Antiviral components%Separation and purification%Stability
为进一步了解小链霉菌 Yn168代谢产物中抗病毒活性物质的化学本质,为其作用机理的研究和产品开发提供依据,对该小链霉菌产生的抗病毒物质的活性组分进行了分离纯化及稳定性研究。经过乙酸乙酯萃取、三氯乙酸沉淀、SephadexG-75柱层析、聚丙烯酰胺凝胶电泳( SDS-PAGE),证明小链霉菌 Yn168发酵液中的活性成分为2个组分的蛋白质Ⅰ168和Ⅱ168,分子量分别为34,22 kDa。稳定性研究表明,抗病毒蛋白在温度超过60℃、pH值小于6或大于8以及紫外线照射时间超过8h的条件下,抗病毒活性均明显下降。所以,该小链霉菌的抗病毒活性成分为2个组分的小分子蛋白质,适于在较低温度、酸碱度接近中性及避光条件下保存和使用。
為進一步瞭解小鏈黴菌 Yn168代謝產物中抗病毒活性物質的化學本質,為其作用機理的研究和產品開髮提供依據,對該小鏈黴菌產生的抗病毒物質的活性組分進行瞭分離純化及穩定性研究。經過乙痠乙酯萃取、三氯乙痠沉澱、SephadexG-75柱層析、聚丙烯酰胺凝膠電泳( SDS-PAGE),證明小鏈黴菌 Yn168髮酵液中的活性成分為2箇組分的蛋白質Ⅰ168和Ⅱ168,分子量分彆為34,22 kDa。穩定性研究錶明,抗病毒蛋白在溫度超過60℃、pH值小于6或大于8以及紫外線照射時間超過8h的條件下,抗病毒活性均明顯下降。所以,該小鏈黴菌的抗病毒活性成分為2箇組分的小分子蛋白質,適于在較低溫度、痠堿度接近中性及避光條件下保存和使用。
위진일보료해소련매균 Yn168대사산물중항병독활성물질적화학본질,위기작용궤리적연구화산품개발제공의거,대해소련매균산생적항병독물질적활성조분진행료분리순화급은정성연구。경과을산을지췌취、삼록을산침정、SephadexG-75주층석、취병희선알응효전영( SDS-PAGE),증명소련매균 Yn168발효액중적활성성분위2개조분적단백질Ⅰ168화Ⅱ168,분자량분별위34,22 kDa。은정성연구표명,항병독단백재온도초과60℃、pH치소우6혹대우8이급자외선조사시간초과8h적조건하,항병독활성균명현하강。소이,해소련매균적항병독활성성분위2개조분적소분자단백질,괄우재교저온도、산감도접근중성급피광조건하보존화사용。
In order to understand the chemical nature of the antiviral substances from Streptonyces parvus Yn168,and to provide the reference for its mechanism research and product development,antiviral component pro-duced by Streptonyces parvus Yn168 were isolated and its stability were studied. By extracting in ethyl acetate,pre-cipitating with trichloroacetic acid,SephadexG-75 column chromatography and polyacrylamide gel electrophoresis (SDS-PAGE),two ingredients of active protein Ⅰ168 and Ⅱ168 with molecular weight of 34,22 kDa from fermenta-tion broth of Streptonyces parvus Yn168 were isolated. Stability studies showed that the antiviral activity of the pro-tein was decreased significantly at a temperature above 60 ℃,and at a pH value below 6 or above 8,or under the UV irradiation over 8 h. So,the antiviral ingredients include two components of small protein,suitable at lower tem-perature,near neutral pH value,and also in the condition of avoiding light for its preservation and uses.