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RISS 인기검색어
- 검색키워드
- 저자 : Soumya Majumder (검색결과 2 건)
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Metabolomics affirms traditional alcoholic beverage raksi as a remedy for high-altitude sickness
Soumya Majumder,Arindam Ghosh,Sourav Chakraborty,Sumedha Saha,Malay Bhattacharya 한국식품연구원 2021 Journal of Ethnic Foods Vol.8 No.-
Raksi, a fermented distilled alcoholic beverage, is an ethnic drink consumed in high altitude regions of Singalila Ridge of the Himalayas and in adjoining high altitude places in Nepal, northern and north eastern part of India and Tibetan plateau. Like jaanr, tongba, nigar, chhyang, and other fermented ethnic beverages, raksi is considered as an element of ethnopharmacology of high altitude with claims of medicinal properties. An ethnobiological survey was done in the study area prior to collection and identification of raksi samples. In this research, two raksi samples (khokim raksi and chimphing raksi) of Singalila Ridge of the Himalayas were investigated by metabolite profiling using gas chromatography-mass spectrometry analysis. Results of the experiment showed presence of several respiratory protective, cardioprotective, neuroprotective, anti-inflammatory, and antioxidant components which have properties to prevent various high altitude illnesses. Moreover, large quantities of bioactive terpenoids, fatty acid derivatives, coumarins, and peptides were detected whose chemotaxonomy and biosynthesis pathways were further studied. This metabolomics investigation not only affirmed Raksi as a remedy for high-altitude sickness but also helped in understanding the importance of this type of ethnic foods in high altitude ethnoecology. This research on raksi in the fields of ethnobiology and metabolomics is a cumulative approach which has opened the door for in-depth investigations on similar ethnic foods. However, further experiments on raksi are surely needed in ethnobiology, microbiology, biochemistry, and food technology.
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Samudra Prosad Banik,Swagata Pal,Shakuntala Ghorai,Sudeshna Chowdhury,Rajib Majumder,Soumya Mukherjee,Suman Khowala 한국생물공학회 2012 Biotechnology and Bioprocess Engineering Vol.17 No.5
Cellobiase (E.C. 3.2.1.21), is a widely exploited industrial glycosidase with a major role in biofuel industry. Its stability and shelf life are major bottlenecks in achieving a superior formulation for industry. In the filamentous fungus Termitomyces clypeatus, the enzyme is secreted in a co-aggregated form with sucrase; the separation of this co-aggregation results in substantial loss of the enzyme’s activity. The aim of the present study was to examine the mode of aggregation of the secreted cellobiase-sucrase coaggregate and its role in the stabilization of cellobiase. Transmission electron microscopy and dynamic light scattering of purified co-aggregates revealed reversible, concentration driven self-aggregation of the extracellular enzymes to form larger entities. However, the intracellular enzyme aggregates were rigid,non-interacting, and possessed a higher percentage of disulphide bonds. Circular dichroic spectra of the two coaggregates indicated no significant difference in secondary structures. Self-association increased the stability of extracellular aggregates towards heat by 1.5 fold, SDS by 4 ~ 7 fold, and chaotropic agents, by 1.5 ~ 2 fold, than the intracellular counterpart. The Km of extracellular aggregate varied between 0.29 and 0.45 mM as a result of spontaneous aggregation and disaggregation, whereas that of intracellular aggregate was 0.22 mM irrespective of its concentration status. In situ detection of cellobiase in native PAGE revealed two activity bands of the extracellular enzyme, which indicated a minimum of two active dissociated aggregate species, as compared to a single band for the intracellular enzyme. These studies are believed to improve the understanding of aggregation of the fungal glycosidases, which remains to be a blackbox, to increase the efficacy of these enzymes. Cellobiase (E.C. 3.2.1.21), is a widely exploited industrial glycosidase with a major role in biofuel industry. Its stability and shelf life are major bottlenecks in achieving a superior formulation for industry. In the filamentous fungus Termitomyces clypeatus, the enzyme is secreted in a co-aggregated form with sucrase; the separation of this co-aggregation results in substantial loss of the enzyme’s activity. The aim of the present study was to examine the mode of aggregation of the secreted cellobiase-sucrase coaggregate and its role in the stabilization of cellobiase. Transmission electron microscopy and dynamic light scattering of purified co-aggregates revealed reversible, concentration driven self-aggregation of the extracellular enzymes to form larger entities. However, the intracellular enzyme aggregates were rigid,non-interacting, and possessed a higher percentage of disulphide bonds. Circular dichroic spectra of the two coaggregates indicated no significant difference in secondary structures. Self-association increased the stability of extracellular aggregates towards heat by 1.5 fold, SDS by 4 ~ 7 fold, and chaotropic agents, by 1.5 ~ 2 fold, than the intracellular counterpart. The Km of extracellular aggregate varied between 0.29 and 0.45 mM as a result of spontaneous aggregation and disaggregation, whereas that of intracellular aggregate was 0.22 mM irrespective of its concentration status. In situ detection of cellobiase in native PAGE revealed two activity bands of the extracellular enzyme, which indicated a minimum of two active dissociated aggregate species, as compared to a single band for the intracellular enzyme. These studies are believed to improve the understanding of aggregation of the fungal glycosidases, which remains to be a blackbox, to increase the efficacy of these enzymes.
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