The increased demand for microbial originated Industrial enzymes especially lipases which have received least priority till last one and half decades and gained lots of importance in recent days owing to their applications in wide variety of fields such as food, dairy, pharmaceutical, detergent, textile, oleo-chemical, perfume and cosmetic industries etc., has lead to the identification of novel enzymes from new sources with unique properties. The present review mainly focuses on various currently available screening methods for identification of lipase producers.

Breast cancer is one of the most common malignancies in women and the leading cause of cancer mortality. Hypercholesterolemia and obesity are potential risk factors for the incidence of breast cancer, and their detection can enhance cancer prevention. In this paper, we discuss the current state of investigations on the importance of lipoproteins, such as low denisity lipoproteins (LDL) and high density lipoproteins (HDL), and cholesterol transporters in the progression of breast cancer, and the therapeutic strategies to reduce breast cancer mortality. Although some research has been unsuccessful at uncovering links between the roles of lipoproteins and breast cancer risk, major scientific trials have found a straight link between LDL levels and incidence of breast cancer, and an inverse link was found between HDL and breast cancer development. Cholesterol and its transporters were shown to have significant importance in the development of breast cancer in studies on breast cancer cell lines and experimental mice models. Instead of cholesterol, 27-hydroxycholesterol, which is a cholesterol metabolite, is thought to promote propagation and metastasis of estrogen receptor-positive breast cancer cell lines. Alteration of lipoproteins via oxidation and HDL glycation are thought to activate many pathways associated with inflammation, thereby promoting cellular proliferation and migration, leading to metastasis while suppressing apoptosis. Medications that lower cholesterol levels and apolipoprotein A-I mimics have appeared to be possible therapeutic agents for preventing excessive cholesterol’s role in promoting the development of breast cancer.

Aloe vera, a succulent plant that grows in arid and subtropical climates is best known for its medicinal properties and is used in Ayurvedic, Homoeopathic and Allopathic streams of medicine. It has been in use for a long time by people of varied cultures and traditional uses include applications to reduce perspiration, oral dosing for diabetes and to get rid of a range of gastrointestinal ailments. It is also used to treat burn wounds, minor cuts, genital herpes, and seborrheic dermatitis. The leaves of this wonderful medicinal plant contain numerous vitamins, minerals, natural sugars, enzymes, amino acids, and as well rich in various bioactive compounds that exhibit emollient, purgative, anti-inflammatory, antioxidant, antimicrobial, anti-helmenthic, antifungal, aphrodisiac, antiseptic and cosmetic values. Many cosmetic industries widely use this plant owing to its healing and nourishing properties.  Keywords: Aloe vera, Medicinal Uses, bioactive compounds, Cosmetic industries

Proteases constitute most important enzymes owing to their wide variety of functions and have immense applications in various industries viz., medical, pharmaceutical, biotechnology, leather, detergent, and food industries. Despite of their wide spread occurrence in various sources, microorganisms present remarkable potential for proteolytic enzymes production due to their extensive biochemical diversity and susceptibility to genetic manipulation. The present study was aimed at isolating alkaline protease producing fungal members from dairy form effluents, designing the process variables for maximizing the protease production and determining the fibrinolytic potential of the partially purified alkaline protease. To achieve the specified objectives, the dairy form effluent was processed for the isolation of proteolytic fungi using suitable microbiological medium. All the fungal isolates were screened for their protease producing ability and the isolate showing highest alkaline protease production was selected for further studies. Optimization of different fermentative variables like carbon, nitrogen sources, pH, temperature and incubation period were carried out to enhance enzyme production. Ammonium sulphate fractionation was employed to partially purify the enzyme following which its fibrinolytic potential was determined. Based on morphological and microscopic studies, the selected fungal isolate was identified as Aspergillus niger. Optimization studies using OVAT (one variable at a time) method revealed an enhanced protease production in the presence of fructose as additional carbon source and ammonium sulphate as nitrogen source. The optimum incubation period, temperature and pH for enzyme production by the selected fungal isolate was found to be 92 h, 50°C and 10, respectively. The partially purified alkaline protease was efficient in the removal of blood stains emphasizing its fibrinolytic ability. An alkaline protease producing Fungal sp. was screened and isolated from dairy form effluent and it was found to be efficient in the removal of blood stains proving its fibrinolytic potential. Enzymes produced from microorganisms that can survive under extremes of pH could be particularly useful for commercial applications under high alkaline conditions.

A cold active lipase producing mesophilic fungus was isolated from Palm Oil Mill Effluent (POME) dump sites and identified by 28S rRNA molecular identification studies as Emericella nidulans NFCCI 3643. The BLAST P search with the sequence of the purified cold active lipase obtained by MALDI-TOF/MS analysis revealed that the protein is a hypothetical protein from Emericella nidulans with a gi number 67522685. Search of Lipase Engineering Database (LED) for this protein sequence revealed that this protein belongs to Candida antarctica lipase A like super family and to Aspergillus lipase like homologous family of class Y lipases. In the present study, a 3D structure of EnL A (Emericella nidulans lipase A) was built using homology modeling, the model was further optimized by molecular dynamic simulations and the optimized model was then docked with natural substrates. Secondary structure analysis of EnL A showed 37.11% of its content to be alpha helix making it stable for three dimensional structure modeling. Homology model of EnL A was constructed using the X-ray structure of Candida antarctica Lip A (3 guu.1.A) as a template with which EnL A showed 32.77% sequence identity. The stereo chemical quality and side chain environment of the model was validated by Ramachandran plot, ERRAT and Verify 3D. Natural substrates like tributyrin and trioctanoin were docked in to the optimized 3D model to further investigate the ligand-enzyme interactions.