Mushroom Research Centre, Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia.
J Microbiol Methods. 2011 Oct;87(1):56-63. doi: 10.1016/j.mimet.2011.07.005. Epub 2011 Jul 23.
Mushrooms are considered as important source of biologically active compounds which include low-molecular-mass protein/peptides (LMMP). In this study, we attempted to profile the LMMP from Lignosus rhinocerus, a wild medicinal mushroom, grown by static cultures (SC) and in stirred tank reactor (STR). Crude water extract (CWE) and protein fractions were profiled using H50 ProteinChip® arrays and SELDI-TOF-MS. Three protein peaks of 5.8, 6.9 and 9.1 kDa were found to be common to spectra of L. rhinocerus CWE from both culture conditions. Partial protein purification has resulted in detection of more peaks in the spectra of protein fractions. For protein fractions of L. rhinocerus cultured in STR, most peaks were observed in the range of 3-8 kDa whereas some peaks with molecular mass up to 14.3 kDa were noted in spectra of protein fractions from SC. Our results have demonstrated the optimization of profiling method using SELDI-TOF-MS for fungal LMMP.
蘑菇被认为是含有低分子质量蛋白质/肽（LMMP）等生物活性化合物的重要来源。在这项研究中，我们尝试对由静态培养（SC）和搅拌槽反应器（STR）培养的野生药用蘑菇红栓菌中的 LMMP 进行分析。采用 H50 蛋白质芯片和 SELDI-TOF-MS 对粗水提取物（CWE）和蛋白质级分进行了分析。结果发现，来自两种培养条件的红栓菌 CWE 的图谱中存在 5.8、6.9 和 9.1 kDa 的 3 个共同的蛋白质峰。部分蛋白质纯化后，在蛋白质级分的图谱中检测到更多的峰。对于在 STR 中培养的红栓菌的蛋白质级分，大多数峰出现在 3-8 kDa 的范围内，而在 SC 蛋白质级分的图谱中则观察到一些高达 14.3 kDa 的峰。我们的结果表明，SELDI-TOF-MS 用于真菌 LMMP 的分析方法得到了优化。
