A Comprehensive Review on Biology, Genetic Improvement, Agro and Process Technology of German Chamomile (Matricaria chamomilla L.).

German chamomile (M. chamomilla) is recognized as a star herb due to its medicinal and aromatic properties. This plant is found across a wide range of climatic and soil conditions. Both the flower heads and blue essential oils of German chamomile possess several pharmacological properties of an anti-inflammatory, antimicrobial, antiseptic, antispasmodic and sedative, etc., nature, which makes it a highly sought after herb for use in many pharma and aroma industries. Chamomile tea, prepared from its flower heads, is also a well-known herbal tea for mind and body relaxation. Though it is a high-demand herb, farmers have not adopted this plant for large scale cultivation as a crop, which could improve their livelihood, due to the high cost in flower heads harvesting, loss in over mature and immature flower heads picking during harvesting, unavailability of varieties and agrotechnologies for machine harvesting, a lack of efficient process development of oil extraction and in the lack of improved stable varieties. There are many studies that have reported on the phytochemistry and pharmacological uses of chamomile, which further explore its importance in the medicine industry. Several studies are also present in the literature on its cultivation practices and plant ecology. However, studies on breeding behavior, genetic improvement, varietal development and mechanical harvesting are scarce in German chamomile. Hence, keeping in mind various aspects of farmers' and researchers' interest, earlier reports on taxonomy, floral biology, processing of oil extraction, active constituents, uses, agronomy, breeding challenges and opportunities in German chamomile are summarized in this review.

Molecular modeling and docking of recombinant HAP-phytase of a thermophilic mould Sporotrichum thermophile reveals insights into molecular catalysis and biochemical properties.

A thermostable and protease-resistant HAP-phytase of Sporotrichum thermophile was over-expressed in Pichia pastoris X-33. Purified recombinant phytase displayed all its biochemical properties similar to wild type. Molecular modeling and docking of phytase with various substrates showed differential binding patterns with GoldScore values ranging from 40.61 to 79.78. Docking with different substrates revealed strong binding affinity with ATP and phytic acid, while the lowest with AMP and phosphoenol pyruvate. This was further confirmed using biochemical assays, as the recombinant enzyme displayed broad substrate specificity. Docking with inhibitors also showed differential binding with GoldScore values ranging from 22.94 (2,3-butanedione) to 85.72 (myo-inositol hexasulphate). Validation using biochemical analysis revealed that both 2,3-butanedione and phenyl glyoxal inhibited the phytase activity significantly. Furthermore, presence of inorganic phosphate in the reaction mixture also inhibited the phytase activity, as there was no activity at and beyond 0.8 mM. Docking of phytase with metavanadate showed binding at the same atom in the active-site where the substrate i.e. phytic acid binds. Vanadium incorporation resulted in the catalytic conversion of phytase into a peroxidase with concomitant inhibition of phytase activity. Peroxidase activity was high in acidic range and the product formation showed correlation with reaction time. Furthermore, molecular modeling and docking of recombinant HAP-phytase of a thermophilic mould S. thermophile reveals insights into molecular catalysis that is validated by the biochemical properties.

Mixed Substrate Fermentation for Enhanced Phytase Production by Thermophilic Mould Sporotrichum thermophile and Its Application in Beneficiation of Poultry Feed.

The optimum values of the critical variables determined by the central composite design of response surface methodology (RSM) for maximum phytase production (1881.26 U g(-1) dry mouldy residue (DMR)) by Sporotrichum thermophile are 2.5 % Tween 80, 1.0 % yeast extract and 48 h of incubation period. Phytase production in the mixed substrate (sugarcane bagasse and wheat bran) fermentation enhanced 11.6-fold over the initial production as a consequence of optimization. Phytase titres are sustainable in flasks, trays and column bioreactor (1796 to 2095 U g(-1) DMR), thus validating the model and the process for large-scale phytase production. When the yeast extract was replaced with corn steep liquor (2 % w/v), a sustained enzyme titre (1890 U g(-1) DMR) was attained, making the process cost-effective. Among all the detergents, Tween 80 supported a higher phytase production than others. The enzyme efficiently liberated nutritional components from poultry feed (inorganic phosphate, soluble protein and reducing sugars) in a time-dependent manner.