No abstract

Microplastic bers (MF) are released from synthetic textiles during washing and end up in the wastewater. Similarly, silver nanoparticles (AgNP), incorporated in textiles as antimicrobial agents, are released in washing machines, also reaching the wastewater treatment plants. Therefore, both MF and AgNP co-exist in the environment, and enter the soil compartment mainly via the application of biosolids.Yet, the combined effect of MF and AgNP has not been studied. Here, we assessed the effects of polyester MF (0.01% DW) on the toxicity of AgNP (32, 100, 320, 1000, 3200 mg Ag/kg) and AgNO 3 (12.8, 32, 80, 200, 500 mg Ag/kg) to the earthworm Eisenia andrei and the enchytraeid Enchytraeus crypticus. The exposure to MF caused a decrease in the number of juveniles and changed the biochemical composition of earthworms. Moreover, the presence of MF increased the toxicity of AgNP to earthworm reproduction (EC50 = 165 mg Ag/kg) when compared to AgNP exposure alone (EC50 = 450 mg Ag/kg), but did not alter the toxicity of AgNO 3 (EC50 = 40 mg Ag/kg). For enchytraeids, no signi cant difference in Ag toxicity could be detected when MF was added to the soil for both AgNP and AgNO 3 . Overall, Ag bioaccumulation was not affected by MF, with the exception of a decrease in earthworm body concentration at the highest Ag soil concentration (3200 mg Ag/kg). Our results suggest that the presence of MF in the soil compartment may be a cause of concern, and that the joint exposure to Ag may be deleterious depending on the Ag form, organism and endpoint. The present work provides the rst evidence that a realistic MF concentration in soil lowers AgNP concentration necessary to provoke reproductive impairment in earthworms. The in uence of MF on risk assessment of AgNP should be considered.

The objective of the study described the importance of L-asparaginase and its importance in the field of medicine. Different types of enzymes are produced based on the adaptation to the environment where the living organisms live to tune the metabolic pathways according to their adapted changes. The enzymes present in various organs are produced by many cell types in multicellular organisms. Except ribosomes all other known enzymes are proteinaceous in nature. L-asparaginase is a potential therapeutic agent for acute lymphoblastic leukemia (ALL) and chronic myelogenous leukemia which is approved by FDA & WHO. L-asparaginase catalyzes the deamination of L-asparagine to L-aspartic acid & ammonia. Unlike normal cells, malignant cells require large amount of L-asparagine for protein synthesis and cell division. From this background the present review is an effort to gather the information on the mechanism, sources, molecular details and application of L-asparaginase enzyme.

In recent years, there has been a phenomenal increase in the use of alkaline proteases as industrial catalysts. The aim of this work was to isolate potent fungal strain from the agricultural field of Gulbarga region of India, for the production of alkaline protease by utilizing the agricultural by products viz, red and green gram and Bengal gram as substrate under submerged fermentation process. Optimization of fermentation process parameters such as substrate (Red gram husk, green gram husk and Bengal gram husk) utilization, utilization, temperature, pH and incubation period for alkaline protease production was carried out. The maximum production of alkaline protease by Trichoderma VPG 12 was found at pH 8, temperature 35 °C, incubated for 120 h. But the activity of the enzyme could also be seen in a wide range of pH (5-9) and temperature (20-40 °C). With all these properties, the strain can be considered for industrial grade production of alkaline protease.

L-asparaginase (L-asp) is used in the treatment of acute lymphocytic leukemia (ALL). L-asp catalyzes the L-asp into ammonia and L-aspartic acid through deamination. The formed ammonia finds to be toxic to the organism. Therefore, the search for less cytotoxic anti-proliferative L-asp is of great importance. Because of its cost effectiveness, consistency, and easiness of process control, microbial L-asparaginase is chosen over plant or animal enzymes. L-asp enzyme which was studied in the article was isolated from a newly discovered bacteria Myroides gitamensis. The biochemical characteristics and anti-proliferative, cytotoxic effect of purified L-asp were studied in order to develop safer biochemically stable anti-leukemia medication. To provide comprehensive information on the characteristics of the isolated L-asparaginase enzyme analytical tools were utilized, including cancer cell lines, brine shrimps, enzyme reactions etc. MOLT-4 and K-562 cell lines showed an IC50 value of 91.41 IU/mL and 77.42 IU/mL, respectively. Cytotoxicity activity of L-asp on Artemia salina showed that at 24 hours (LC50 value of 217.0 µg/mL) and toxic at 48 hours (LC50 value of 126.4µg/ml).