Protein-Based Films and Coatings for Food Industry Applications.

Food packaging is an area of interest not just for food producers or food marketing, but also for consumers who are more and more aware about the fact that food packaging has a great impact on food product quality and on the environment. The most used materials for the packaging of food are plastic, glass, metal, and paper. Still, over time edible films have become widely used for a variety of different products and different food categories such as meat products, vegetables, or dairy products. For example, proteins are excellent materials used for obtaining edible or non-edible coatings and films. The scope of this review is to overview the literature on protein utilization in food packages and edible packages, their functionalization, antioxidant, antimicrobial and antifungal activities, and economic perspectives. Different vegetable (corn, soy, mung bean, pea, grass pea, wild and Pasankalla quinoa, bitter vetch) and animal (whey, casein, keratin, collagen, gelatin, surimi, egg white) protein sources are discussed. Mechanical properties, thickness, moisture content, water vapor permeability, sensorial properties, and suitability for the environment also have a significant impact on protein-based packages utilization.

Binding of JAB1/CSN5 to MIF is mediated by the MPN domain but is independent of the JAMM motif.

Macrophage migration inhibitory factor (MIF) binds to c-Jun activation domain binding protein-1 (JAB1)/subunit 5 of COP9 signalosome (CSN5) and modulates cell signaling and the cell cycle through JAB1. The binding domain of JAB1 responsible for binding to MIF is unknown. We hypothesized that the conserved Mpr1p Pad1p N-terminal (MPN) domain of JAB1 may mediate binding to MIF. In fact, yeast two hybrid (YTH) and in vitro translation/coimmunoprecipitation (CoIP) analysis showed that a core MPN domain, which did not cover the functional JAB1/MPN/Mov34 metalloenzyme (JAMM) deneddylase sequence, binds to MIF comparable to full-length JAB1. YTH and pull-down analysis in conjunction with nanobead affinity matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry demonstrated that MIF(50-65) and MPN are sufficient to mediate MIF-JAB1 interaction, respectively. Finally, endogenous CoIP of MIF-CSN6 complexes from mammalian cells demonstrated that MPN is responsible for MIF-JAB1 binding in vivo, and, as CSN6 does not contain a functional JAMM motif, confirmed that the interaction does not require JAMM.