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New Developments in Oral Insulin Delivery
Published in Emmanuel Opara, Controlled Drug Delivery Systems, 2020
Alec Jost, Mmesoma Anike, Emmanuel Opara
The GI tract maintains a delicate biochemical balance to promote digestion without causing injury to the bowel. Under physiologic conditions, enzymes, specifically proteases, have potential activity against components of living tissue but the body uses counterenzymes and inhibitory factors to prevent unintentional damage. By isolating these counterregulatory compounds from plants and other animals and delivering them in conjunction with orally dosed peptide drugs, researches are able to reduce the rate of peptide degradation and improve oral administration of therapeutic peptides. Enzymes which are known to degrade insulin include trypsin, chymotrypsin, and insulin-degrading enzyme (Durham et al. 2015; Duckworth et al. 1998). Trypsin inhibitors are present in a number of biological mediums including human serum (alpha1-antitrypsin), bovine pancreas (aprotinin), and soybeans (Bowman-Birk trypsin inhibitor, Kunitz soybean trypsin inhibitor, etc.). In the pursuit of an oral administration of insulin, protease inhibitors specific to enzymes involved in insulin degradation are either conjugated directly to insulin or included in a biomaterial construct, potentially increasing the lifetime and consequent probability of absorption of insulin in the GI tract. Protease inhibitors commonly used for oral peptide delivery are included in Table 12.3.
PolyHIPEs for Separations and Chemical Transformations: A Review
Published in Solvent Extraction and Ion Exchange, 2019
Kathryn M. L. Taylor-Pashow, Julia G. Pribyl
Another separations application that has seen extensive use of polyHIPE materials in recent years is the area of protein purification. Unlike the majority of the polyHIPE resins used for metal complexation or ion exchange that were primarily styrene-based foams, the majority of the polyHIPE materials used for protein purification are based on glycidyl methacrylate backbones. The earliest such report of polyHIPEs for protein purification came from Krajnc and coworkers, who prepared polyHIPE monoliths from co-polymerization of glycidyl methacrylate and ethylene glycol dimethacrylate.[28] The epoxy groups on the monomer remained unreacted during the polymerization, and they were then used to further functionalize the material through reaction with diethylamine. The amine functionalization of the material introduced weak anion-exchange groups, which were then used for the protein purification. Chromatographic evaluation was performed using a standard protein mixture containing myoglobin, conalbumin, and trypsin inhibitor. While the dispersion was slightly higher in the polyHIPE samples compared to commercially available materials, the separation was still acceptable.
Modeling of growth kinetics for an isolated marine bacterium, Oceanimonas sp. BPMS22 during the production of a trypsin inhibitor
Published in Preparative Biochemistry and Biotechnology, 2018
B. S. Harish, Kiran Babu Uppuluri
Oceanimonas sp. BPMS22 was isolated for the production a trypsin inhibitor. The proteinaceous trypsin inhibitor of approximately 30 KDa was purified to homogeneity. It has shown a potent in vitro anticoagulant and anticancer activity (this work was accepted by Marine biotechnology, 2018). The major objective of this work is to enhance the production by selecting a suitable medium and to determine the growth and production parameters using kinetic models. In the present work, various media were screened for PI production. Further carbon and nitrogen sources were screened and optimized for the product formation. Gompertz, logistic, and Richards models were compared to estimate the growth parameters. Similarly, production parameters were determined using a kinetic model for product formation during the non-growing phase.
Evaluation of nutritional and medicinal potential of defatted Sapindus mukorossi seed kernel
Published in Preparative Biochemistry & Biotechnology, 2022
Revati S. Chavan, Virendra K. Rathod
According to the relative digestibility studies, the digestibility of proteins was 58.3 ± 0.92%. It is comparable to the trypsin inhibitor activity of defatted sapindus seed kernel protein isolate. Protein’s interaction with other proteins or carbohydrates and phenolic also affects digestibility. Carbohydrates or phenolic shows milliard reaction with proteins resulting in covalent linkage which is difficult to digest by proteases.[21] In the present study, as the results of trypsin inhibitor activity and digestibility are analogous, it can be concluded that interactions of proteins with other components in the sample are negligible.