Agarases (agarose 4-glycanohydrolase; EC 3.2.1.81) are class of enzymes that belong to glycoside hydrolase (GH) family capable of hydrolyzing agar. Their classification depends on hydrolysis pattern and product formation. Among all the agarases, β-agarases and the oligosaccharides formed by its action have fascinated quite a lot of industries. Ample of β-agarase genes have been endowed from marine sources such as algae, sea water, and marine sediments, and the expression of these genes into suitable host gives rise to recombinant β-agarases. These recombinant β-agarases have wide range of industrial applications due to its improved catalytic efficiency and stability in tough environments with ease of production on large scale. In this review, we have perused different types of recombinant β-agarases in consort with their molecular, physiochemical, and kinetic properties in detail and the significant features of those agarases are spotlighted. From the literature reviewed after 2010, we have found that the recombinant β-agarases belonged to the families GH16, GH39, GH50, GH86, and GH118. Among that, GH39, GH50, and GH86 belonged to clan GH-A, while the GH16 family belonged to clan GH-B. It was observed that GH16 is the largest polyspecific glycoside hydrolase family with ample number of β-agarases and the families GH50 and GH118 were found to be monospecific with only β-agarase activity. And, out of 84 non-catalytic carbohydrate-binding modules (CBMs), only CBM6 and CBM13 were professed in β-agarases. We witnessed a larger heterogeneity in molecular, physiochemical, and catalytic characteristics of the recombinant β-agarases including molecular mass: 32-132 kDa, optimum pH: 4.5-9, optimum temperature 16-60 °C, K M : 0.68-59.8 mg/ml, and V max : 0.781-11,400 U/ mg. Owing to this extensive range of heterogeneity, they have lion's share in the multibillion dollar enzyme market. This review provides a holistic insight to a few aspects of recombinant β-agarases which can be referred by the upcoming explorers to this area.

Background: Survivin, smallest Inhibitor of Apoptosis Protein (IAP) mediates apoptosis pathway and cell cycle is tumor specific and therapeutic target for cancer research. Breast cancer is a dreadful disease with greater mortality rate, commonly in women globally. Aim: This study was undertaken to investigate the effect of indigenous Plant drugs by in-silico determination of antagonist for Survivin protein that was up regulated in breast cancer. Materials and Methods: The 3D structure of Survivin protein was retrieved from PDB (Protein Data Bank). Plant compounds were retrieved from NPACT (Naturally occurring Plant based Anti-Cancerous Target) database and converted into 3D- PDB format using Open babel software. Based on the active sites we have screened the essential plant compound as an effective binder against modelled protein using iGEMDock 2.1. Results and conclusion: The lead compound of plant as well as plant protein molecule would be scaled out on the basis of binding efficiency. Remangilones A showed greater interaction effect with Total energy (-121.465kcal mol-1). However, further in-vivo investigation is essential for the confirmation of drug efficacy and bio-compatibility.

Medicinal plant extracts are known to possess breast cancer antidote. The present investigation is focused on anticancer efficacy of various parts of Annona squamosa. The organic (ethanol) extracts from various parts of Annona squamosa were prepared using soxhlet apparatus and tested for in vitro anticancer efficacy on Breast cancer cell line MCF-7 by MTT (3-(4, 5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) assay. The results obtained from MTT assay showed that the inhibitory concentration values of bark, peel and seed were found to be approximately 20, 30 and 10 μg/ml, respectively The ethanolic seed extract had high anticancer activity with IC50 value of 10 ug/ml, reveals that A. squamosa inhibits the proliferation of MCF-7 by inducing apoptosis. The plant investigated has anti-cancer activity; hence further studies should be carried out for the isolation of the lead molecules from the parts of the plant to treat the breast cancer.

Coproduction of multienzymes from single potential microbe has captivated contemplation in industries. Bacterial strain, Halomonas meridiana VITSVRP14, isolated from seaweed was labored to produce amylase, agarase and xylanase conjointly using submerged fermentation. The optimum production conditions clinched by classical optimization were: pH 8; 1.5% inoculum; 24 h incubation, 40 °C; 8% NaCl (sodium chloride); 1% lactose and NaNO3 (sodium nitrate). The preponderant variables (pH, temperature, lactose) and their interaction effect on enzyme production were studied by Plackett-Burman design and Response Surface Methodology (RSM). There were 3.29, 1.81 and 2.08 fold increase in enzyme activity with respect to agarase, amylase and xylanase after optimization against basal medium. After 24 h of enzymatic treatment, the saccharification rates of the coproduced enzyme mixture were 38.96% on rice bran, 49.85% on wheat bran, 61.2% on cassava bagasse and 57.82% on corn cob. Thus, the coproduced enzyme mixture from a bacterium with halotolerance is plausible in pretreated lignocellulose degradation. The ability of this single microbe Halomonas meridiana VITSVRP14, in coproducing agarase, amylase and xylanase give the nod for its application in biomass saccharification by subsiding cost, energy and time involved in the process.