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Interaction of 2-Hydroxyquinoxaline (2-HQ) on Soil Enzymes and Its Degradation: A Review
Venkata Subba Reddy Gangireddygari,Rajasekhar Reddy Bontha,Ju-Yeon Yoon 인간식물환경학회 2020 인간식물환경학회지 Vol.23 No.4
The United Nations project the world population to reach 10 billion by the year 2057. To increase the food of the ever-increasing world population, agrochemicals are indispensable tools to the boon in agriculture production. These agrochemicals are a serious threat to the health of humans, plants, and animals. Agrochemicals are ultimately reached to the main reservoir/sink such as soil and contaminating the groundwater, disturb the soil health and in turn a serious threat to biogeochemical cycling and the entire biosphere. Among agrochemicals, quinalphosis one of the most repeatedly and widely used insecticides in the control of a wide range of pests that attack various crops. Quinalphos is shown to be primarily toxic in organisms by acetylcholinesterase enzyme action. Hydrolysis of quinalphos produces amajor metabolite 2-hydroxyquinoxaline (2-HQ), which has shown secondary toxicity in organisms. 2-HQ is reported to be mutagenic, carcinogenic, growth inhibition and induce oxidative stress in organisms. Quinoline is a heterocyclic compound and structural resemblance of 2-HQ with minor changes, but its degradation studies are enormous compared to the 2-HQ compound. Biotic factors in fate and behavior of 2-HQ in the environment are least studied. 2-HQ interactions with soil enzymes are vary from soil to soil. Based on the toxicity of 2-HQ in our stockpile we need to isolate a handful of microorganisms to treat this persistent metabolite and also other metabolites/compounds.This brief review will be significant from the point of biological and environmental safety.
Enhanced Production and Partial Purification of Glucoamylase from Mutated Bacillus sp. FME
Gudi Satheesh Kumar,Muni Ramanna Gari Subhosh Chandra,Yakasiri Nagasai Sujana,Bontha Rajasekhar Reddy,Yong Lark Choi 한국응용생명화학회 2009 Applied Biological Chemistry (Appl Biol Chem) Vol.52 No.5
In this study, a potent newly-isolated glucoamylase producing actively growing cells of Bacillus sp.FME was subjected to UV irradiation and ethidium bromide (EtBr) mutagenesis. The promising colonies were further screened for glucoamylase production via plate assays and submerged enzyme production at the flask level. Amongst all of the tested colonies, the best mutant, Bacillus sp. FME 2, selected from UV irradiation (20 min) and EtBr (1 mg/mL), was shown to be the most promising. The yield of glucoamylase generated by the mutant strain was approximately 3.0 fold and 1397 U/mL with an incubation period of 24 h, which was larger than the yield generated by the wild-type strain. The glucoamylase was partially purified using ammonium sulphate precipitation followed by gel exclusion chromatography. The enzyme was partially purified 3.0-fold to homogeneity with a final recovery of 66% and a specific activity of 1145 U/mg protein for the mutant strain. The molecular mass was approximately 67.1 kDa, as determined by SDS-PAGE. The active band was observed as a clear colorless area on zymogram analysis, which indicated an absence of glucoamylase isoforms. The results of thin-layer chromatography identified this enzyme as a glucoamylase.
Enhanced Production and Partial Purification of Glucoamylase from Mutated Bacillus sp. FME
Kumar, Gudi Satheesh,Chandra, Muni Ramanna Gari Subhosh,Sujana, Yakasiri Nagasai,Reddy, Bontha Rajasekhar,Choi, Yong-Lark The Korean Society for Applied Biological Chemistr 2009 Applied Biological Chemistry (Appl Biol Chem) Vol.52 No.5
In this study, a potent newly-isolated glucoamylase producing actively growing cells of Bacillus sp. FME was subjected to UV irradiation and ethidium bromide (EtBr) mutagenesis. The promising colonies were further screened for glucoamylase production via plate assays and submerged enzyme production at the flask level. Amongst all of the tested colonies, the best mutant, Bacillus sp. FME 2, selected from UV irradiation (20 min) and EtBr (1 mg/mL), was shown to be the most promising. The yield of glucoamylase generated by the mutant strain was approximately 3.0 fold and 1397 U/mL with an incubation period of 24 h, which was larger than the yield generated by the wild-type strain. The glucoamylase was partially purified using ammonium sulphate precipitation followed by gel exclusion chromatography. The enzyme was partially purified 3.0-fold to homogeneity with a final recovery of 66% and a specific activity of 1145 U/mg protein for the mutant strain. The molecular mass was approximately 67.1 kDa, as determined by SDS-PAGE. The active band was observed as a clear colorless area on zymogram analysis, which indicated an absence of glucoamylase isoforms. The results of thin-layer chromatography identified this enzyme as a glucoamylase.
Enhanced Production and Partial Purification of Glucoamylase from Mutated Bacillus sp. FME
( Gudi Satheesh Kumar ),( Muni Ramanna Gari Subhosh Chandra ),( Yakasiri Nagasai Sujana ),( Bontha Rajasekhar Reddy ),( Yong Lark Choi ) 한국응용생명화학회 2009 Applied Biological Chemistry (Appl Biol Chem) Vol.52 No.5