Abstract: Systems and methods may be used for sign language and gesture identification and capture. A method may include capturing a series of images of a user and determining whether there are regions of interest in an image of the series of images. In response to determining that there is a region of interest in a particular image of the series of images, the method may include determining whether the region of interest includes a gesture movement by the user and determining whether the region of interest includes a sign language sign movement by the user. An image representation of a gesture or a sign may be generated.

Abstract: According to an embodiment, a method to quantify domain-centric risk is disclosed. The method comprises: receiving at least one first input associated with a loss event frequency from at least one first external source in a Risk assessment engine; receiving at least one second input associated with a Loss Magnitude from at least one second external source in the Risk assessment engine; receiving at least one third input associated with a plurality of domain-centric entities from at least one third external source in the Risk assessment engine; analyzing the loss event frequency, the loss magnitude, and the at least one third input to quantify the risk associated with a target domain-centric entity; and generating a risk assessment report for the target domain-centric entity based on the analysis of the loss event frequency, the loss magnitude, and the at least one third input.

Abstract: The present invention relates to a mutant of L-asparaginase enzyme characterized in having high thermostability, pH stability and no glutaminase activity useful for therapeutics and the process of preparing the same. The present invention specifically relates to mutants MTCC 5580, MTCC 5581 and MTCC 5582 characterized in having higher stability, no glutaminase activity etc., to allow their usage in the form of improved protein therapeutics.

Abstract: The present invention relates to a novel mutant of L-asparaginase enzyme characterized in having high thermostability, pH stability and no glutaminase activity useful for therapeutics and the process of preparing the same. The present invention specifically relates to mutant's MTCC 5580, MTCC 5581 and MTCC 5582 characterized in having higher stability, no glutaminase activity etc., to allow their usage in the form of improved protein therapeutics. A thermostable L-asparaginase from P. furiosus was cloned and expressed in E. coli host. The enzyme was engineered at its active site to create three different mutants based on structural and sequence analysis with a E. coli—derived enzyme homologue. The mutants MTCC 5580, MTCC 5581 and MTCC 5582 were tested for their stability, substrate affinity, optimum pH and temperature of activity and cytotoxicity. Based on the studies, all the three enzymes were found thermostable and with no glutaminase activity as compared to other available enzyme EcA II.