Surface energetics to assess influence of biomass-type and biomass-adsorbent interactions in expanded beds.

In integrated bioprocessing applications, expanded bed adsorption (EBA) chromatography presents an opportunity to harvest biomolecules directly from the crude feedstock. However, unfavorable biomass interactions with adsorbent usually leads to fouling, which reduces its protein binding capacity as it alters column hydrodynamics and binding site availability. In this work, a detailed study on biomass adhesion behavior of four different industrially relevant microorganisms on 26 different, most commonly occurring adsorbent surfaces with varying degrees of surface energy and surface charge has been conducted.

High-level fed-batch fermentative expression of an engineered Staphylococcal protein A based ligand in E. coli: purification and characterization.

The major platform for high level recombinant protein production is based on genetically modified microorganisms like Escherichia coli (E. coli) due to its short dividing time, ability to use inexpensive substrates and additionally, its genetics is comparatively simple, well characterized and can be manipulated easily. Here, we investigated the possibilities of finding the best media for high cell density fermentation, by analyzing different media samples, focusing on improving fermentation techniques and recombinant protein production.

Improved biomass and protein production in solid-state cultures of an Aspergillus sojae strain harboring the Vitreoscilla hemoglobin.

The biotechnological value of Aspergillus sojae ATCC 20235 (A. sojae) for production of pectinases in solid-state fermentation (SSF) has been demonstrated recently. However, a common drawback of fungal solid-state cultures is the poor diffusion of oxygen into the fungi that limits its growth and biological productivity.

Cloning and expression of an active aspartic proteinase from Mucor circinelloides in Pichia pastoris.

Background: Extracellular aspartic proteinase (MCAP) produced by Mucor circinelloides in solid state fermentations has been shown to possess milk clotting activity and represents a potential replacement for bovine chymosin in cheese manufacturing. Despite its prospects in the dairy industry, the molecular characteristics of this enzyme remain unknown. This work focuses on MCAP cloning and optimization of heterologous expression in Pichia pastoris, and characterization of the enzyme.