Understanding the relationships between solubility, stability, and activity of silicatein

Abstract

Silicatein is an enzyme that mineralizes environmental precursors to patterned nanomaterials and is found naturally orchestrating the complex and beautiful exoskeletons of marine sponges. To harness this activity for nanomaterial...

Understanding Biomineralization Mechanisms to Produce Size-Controlled, Tailored Nanocrystals for Optoelectronic and Catalytic Applications: A Review

“…201,203,205 No impactful increases in biomineralization activity have been associated with attempts to increase solubility, in fact, some work suggests that even aggregated silicatein is biomineralization active. 204 In order to make silicatein more effective for MoNP biosynthesis, enzyme kinetics should be a target of study. Bawazer et al took a pseudoevolutionary approach via DNA shuffling to generate a library of biomineralization mutants, identifying two mutants with increased binding activity.…”

“…However, these reaction kinetics are still rather slow, and it should be noted that silica precursor species are sparingly soluble, thus making experiments difficult. Recent work by Vigil et al suggests that examining silicatein biomineralization with ceria may be an advantageous approach to kinetics studies in order to avoid the confounding effects of TEOS autohydrolysis in silica production . In order to compensate for the slow kinetics, researchers have strived to increase enzyme solubility via the addition of many different solubility fusion tags, including Trigger-Factor, glutathione, maltose binding protein, and Pro-S2. ,, No impactful increases in biomineralization activity have been associated with attempts to increase solubility, in fact, some work suggests that even aggregated silicatein is biomineralization active …”

Investigating the effect of fusion partners on the enzymatic activity and thermodynamic stability of poly(ethylene terephthalate) degrading enzymes

“…The issue is more acute at the elevated temperatures that enzymes digesting plastics like polyethylene terephthalate (PET) commonly operate, where the need for a flexible active site works in opposition to the requirement for thermal stability 1,2 . Enhanced stability through coupling of enzymes to suitable protein partners has been observed across a variety of enzyme classes acting on soluble substrates [3][4][5] . Despite these successes, the benefits of fusions to enzymes acting at a polymer surface is less clear cut.…”