Immobilization of enzymatic extracts of Portulaca oleracea cv. roots for oxidizing aqueous bisphenol A

Abstract

Water pollution from the release of industrial wastewater is a serious problem for almost every industry. Enzymes from portulaca, Portulaca oleracea cv., have been investigated for their ability to degrade bisphenol A (BPA), one of the well-known estrogenic pollutants. Enzymatic crude extracts from P. oleracea cv. roots were immobilized on aminopropyl-modified glass beads. They maintained BPA metabolic activity over a broad range of pH values and temperatures. The immobilized enzyme was reusable with more than 50 % of its initial activity retained after 12 batch reactions and no loss of activity after storage for 1 month at -30 °C. Thus, the immobilization of extracts from P. oleracea cv. roots is a useful method for removing BPA from industrial wastewater.

Direct immobilization of laccase on titania nanoparticles from crude enzyme extracts of P. ostreatus culture for micro-pollutant degradation

“…2.8 L min -1 mg -1 for free enzyme vs 1.8 L min -1 mg -1 for the immobilized enzyme). These changes are commonly observed in enzyme immobilization studies [9,21,22]. The increase of K m after immobilization can be mainly ascribed to the internal and external limitations, such as mass transfer resistance and limited accessibility of active sites after immobilization.…”

“…In addition, these steps also incur extra downstream processing costs. Ideally, the enzyme purification and stabilization should be achieved simultaneously, and recently a few related techniques have been reported, such as support surface activation [16,21,22], protein-inorganic composite formation [23], and enzyme selfcrosslinking [24][25][26]. As discussed above, the functionalized TiO 2 nanoparticle can be a promising candidate for enzyme immobilization.…”