The role of phosphate in silk fibroin self-assembly: a Hofmeister study.

Silk fibroin is the primary protein component of the threads of silkworm cocoons. Previous work has demonstrated that silk fibroin can self-assemble at solid-liquid interfaces to form dense, nanothin coatings that grow continuously from a substrate surface when exposed to potassium phosphate, a kosmotropic salt. Herein, the role of potassium phosphate in promoting silk fibroin self-assembly in solution and on surfaces is studied and compared to other salts in the Hofmeister series.

Phosphate-Driven Interfacial Self-Assembly of Silk Fibroin for Continuous Noncovalent Growth of Nanothin Defect-Free Coatings.

Silk fibroin is a fiber-forming protein derived from the thread of silkworm cocoons. This biocompatible protein, under the kosmotropic influence of potassium phosphate, can undergo supramolecular self-assembly driven by a random coil to β-sheet secondary structure transition. By leveraging concurrent nonspecific adsorption and self-assembly of silk fibroin, we demonstrate an interfacial phenomenon that yields adherent, defect-free nanothin protein coatings that grow continuously in time, without observable saturation in mass deposition.

One pot clarification and debittering of grapefruit juice using co-immobilized enzymes@chitosanMNPs.

In the present work, enzymes pectinase and naringinase were simultaneously co-immobilized on an eco-friendly chitosan coated magnetic nanoparticles (chitosanMNPs) by cross-linking using chitosan as a macro-molecular cross-linker. The maximum activity recovery of both enzymes in the co-immobilized form was obtained at chitosanMNPs to enzymes ratio of 1:3, 3% cross-linker concentration and 150 min cross-linking time. The synthesized MNPs before and after co-immobilization were characterized using different techniques.