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1.
Braz. J. Pharm. Sci. (Online) ; 58: e20743, 2022. tab, graf
Article in English | LILACS-Express | LILACS | ID: biblio-1420421

ABSTRACT

Abstract Current study compares the Therapeutic/nutra-pharmaceuticals potential and phenolics profile of Pakistani grown Pakistani and Chinese varieties of ginger. Crude yield of bioactive components from the varieties tested, using different extraction solvents including chloroform, ethyl acetate, ether, methanol, ethanol and distilled water. The crude bioactives varied from 14.1-82.5%. The highest extraction yield was noted for Pakistani species. The HPLC analysis revalued significant amounts of phenolics including vanillin, protocatechuic, vanillic, ferulic, sinapinic and cinnamic acids. The highest anti-inflammatory activity was shown by ethanolic extract of Pakistani variety (IC50: 26.5±1.8) whereas Chinese variety exhibited potent anticancer potential against MCF-7 cell line (Inhibition: 91.38 %). The Chinese variety in general showed higher phenolics and anticancer, while the Pakistani exhibited higher anti-inflammatory activity. Pakistani grown ginger and ethanolic extract of Chinese ginger showed highest antimicrobial activity against Pseudomonas aeruginosa 18.0±0.02 & 15.00±0.02 mm respectively. Minimum results obtained with water for both varieties of ginger with range of 7.2±0.22 and 6±0.07 respectively. Moreover, the phenolics composition, anti-inflammatory, antibacterial and anticancer activities of both tested varieties of ginger were notably affected as a function of extraction solvents. Our findings advocate selection of appropriate solvent for recovery of effective phenolic bioactive compounds from ginger verities to support the Nutra-pharmaceutical formulation.

2.
Int J Biol Macromol ; 175: 108-122, 2021 Apr 01.
Article in English | MEDLINE | ID: mdl-33548312

ABSTRACT

Lipases belong to α/ß hydrolases that cause hydrolytic catalysis of triacylglycerols to release monoacylglycerols, diacylglycerols, and glycerol with free fatty acids. Lipases have a common active site that contains three amino acid residues in a conserved Gly-X-Ser-X-Gly motif: a nucleophilic serine residue, an acidic aspartic or glutamic acid residue, and a basic histidine residue. Lipase plays a significant role in numerous industrial and biotechnological processes, including paper, food, oleochemical and pharmaceutical applications. However, its instability and aqueous solubility make application expensive and relatively challenging. Immobilization has been considered as a promising approach to improve enzyme stability, reusability, and survival under extreme temperature and pH environments. Innumerable supporting material in the form of natural polymers and nanostructured materials is a crucial aspect in the procedure of lipase immobilization used to afford biocompatibility, stability in physio-chemical belongings, and profuse binding positions for enzymes. This review outlines the unique structural and functional properties of a large number of polymers and nanomaterials as robust support matrices for lipase immobilization. Given these supporting materials, the applications of immobilized lipases in different industries, such as biodiesel production, polymer synthesis, additives, detergent, textile, and food industry are also discussed.


Subject(s)
Enzymes, Immobilized/chemical synthesis , Lipase/chemistry , Lipase/metabolism , Biocatalysis , Biofuels , Biotechnology/methods , Catalysis , Enzyme Stability , Enzymes, Immobilized/chemistry , Food Industry , Nanostructures/chemistry
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