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New Findings from S.M. Moon and Co-Authors in the Area of Enzymes and Coenzymes Reported (Purification and characterization of a novel fibrinolytic...

July 23, 2014



New Findings from S.M. Moon and Co-Authors in the Area of Enzymes and Coenzymes Reported (Purification and characterization of a novel fibrinolytic alpha chymotrypsin like serine metalloprotease from the edible mushroom, Lyophyllum shimeji)

By a News Reporter-Staff News Editor at Biotech Week -- Investigators discuss new findings in Enzymes and Coenzymes. According to news reporting originating from Gyeonggi Do, South Korea, by NewsRx correspondents, research stated, "A novel fibrinolytic enzyme was purified from Lyophyllum shimeji, a popular edible mushroom in Asia. The enzyme was purified using combination of anion exchange chromatography on a Mono Q 5/5 column and size exclusion gel filtration chromatography on Superdex 200 100/300 column."

Our news editors obtained a quote from the research, "This purification protocol resulted 80.9-fold purification of the enzyme and a final yield of 5.7%. The molecular weight of the purified enzyme was estimated to be 21 kDa by SDS-PAGE and size exclusion gel filtration. The N-terminal amino acid sequence was found to be ITFQSASP, which is dissimilar from that of known fibrinolytic enzymes. The purified enzyme was a neutral protease with an optimal reaction pH and temperature of 8.0 and 37 degrees C, respectively. Enzymatic activity was inhibited by Cu2+ and Co2+. It was also significantly inhibited by PMSF and TPCK. Furthermore, it was found to exhibit a higher specificity for S-7388, a well-known chymotrypsin chromogenic substrate, indicating chymotrypsin like serine metalloprotease. The relative fibrinolytic activity of 5 mu g purified enzyme have two fold more activity than 1 unit/ml of plasmin on fibrin plate. Furthermore, purified enzyme preferentially hydrolyzed the A alpha-chain followed by the B beta- and gamma-chain of fibrinogen, which is precursor of fibrin."

According to the news editors, the research concluded: "Therefore, these data suggests that the fibrinolytic enzyme derived from edible mushroom, L. shimeji, might be useful for thrombolytic therapy and preventing thrombotic disease."

For more information on this research see: Purification and characterization of a novel fibrinolytic alpha chymotrypsin like serine metalloprotease from the edible mushroom, Lyophyllum shimeji. Journal of Bioscience and Bioengineering, 2014;117(5):544-550. Journal of Bioscience and Bioengineering can be contacted at: Soc Bioscience Bioengineering Japan, Osaka Univ, Faculty Engineering, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan. (Elsevier - www.elsevier.com; Journal of Bioscience and Bioengineering - www.elsevier.com/wps/product/cws_home/505516)

The news editors report that additional information may be obtained by contacting S.M. Moon, Korea Inst Planning & Evaluat Technol Food Agr Fo, Anyang Si 431810, Gyeonggi Do, South Korea. Additional authors for this research include J.S. Kim, H.J. Kim, M.S. Choi, B.R. Park, S.G. Kim, H. Ahn, H.S. Chun, Y.K. Shin, J.J. Kim, D.K. Kim, S.Y. Lee, Y.W. Seo, Y.H. Kim and C.S. Kim (see also Enzymes and Coenzymes).

Keywords for this news article include: Asia, Serine, Gyeonggi Do, South Korea, Neutral Amino Acids, Enzymes and Coenzymes

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Biotech Week


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