Search

Reclamation is an effort to repair the damaged mining sector to provide optimal benefits. This review article aims to propose a natural product technology approach to the reclamation of post-coal mining land by increasing the content of soil organic matter so that the post-mining land becomes fertile and can be used for agricultural land. The method used is an observation and literature study. Literature searches were using them ScienceDirect, Scopus, PubMed, and Google Scholar databases. Land-use change of post-mining site to agricultural land provides prospective economic value to the community. However, the land quality of the post-mining area should be improved before food crop production. Tephrosia vogelii is a member of the Papilionoideae subfamily is important for land revegetation. They can fertilize the soil because of mutualistic symbiosis with the bacteria Rhizobium sp. which is capable to fix nitrogen in the soil and hence provide available nitrogen. Thus, the use of post-mining land as agriculture can improve the economy and sustainability as well as protect life and the environment with natural product technology.

Isoniazid (INH) is a drug for the treatment of tuberculosis in patients infected with Mycobacterium tuberculosis. The katG enzyme, or catalase-peroxidase, activates the pro-drug INH that is coded by the katG gene in M. tuberculosis. Mutations of the katG gene in M. tuberculosis are a major INH resistance mechanism. The M. tuberculosis clinical isolate R2 showed INH resistance at a high level of 10 µg/mL. However, the molecular basis for the resistance is unclear. The identification of a mutation in the katG gene of the clinical isolate R2 showed four mutations, i.e., C1061T, G1261 A, G1388T, G2161A, which correspond to the amino acid substitutions T354I, G421S, R463L, and V721M, respectively. The mutant katG gene, along with the wild-type were cloned, expressed and purified. The mutant enzyme showed 86.5% of catalase and 45% of peroxidase activities in comparison to the wild type. The substitutions of T354I and G421S in mutant katG R2 created significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis. The events could be based on the high resistance of the clinical isolate R2 toward INH as the molecular basis.

The mechanism of the positive cardioactive effects induced by verbascoside in the Lagendorff rat heart has been investigated. Isolated rat hearts treated with alpha- or beta-adrenergic agents did not show significant reduction of the positive chronotropism, inotropism and increased coronary perfusion rate mediated by verbascoside. A significant increase in prostacyclin levels (142%) observed following the administration of verbascoside suggests that prostacyclin stimulates formation of cAMP which induces the cardioactivity associated with verbascoside.