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Utilization of Fisheries' By-Products for Functional Foods
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Muhamad Darmawan, Nurrahmi Dewi Fajarningsih, Sihono, Hari Eko Irianto
There are several ways to hydrolyze the fish protein such as chemically hydrolysis, thermal hydrolysis and enzymatic hydrolysis (Zamora-Sillero et al., 2018). Among the methods, chemically hydrolysis using alkali and acid is relatively low cost and simple to operate; thus, the method is widely used at an industrial scale. However, compared to biochemical methods, the chemical and thermal hydrolysis approach is harsher, which caused amino acid profile damage, a loss of nutrients, and produced very heterogeneous peptides due to the nonspecific peptide bond cleaving. Biochemical hydrolysis can be done using endogenous proteolytic enzymes of the fish proteins or using exogenous enzymes. According to Zamora-Sillero et al. (2018), the hydrolyzing process of the fish protein is much more controllable when an exogenous enzyme is used compared to the endogenous enzyme. Moreover, an exogenous enzyme will produce a better homogeneous protein hydrolysate. Therefore, an enzymatic approach is currently considered as the most effective protein hydrolysis method available to produce FPH. Enzyme selection has a key role in hydrolyzing fish protein.
Constitutive Host Resistance
Published in Julius P. Kreier, Infection, Resistance, and Immunity, 2022
Cells of the mononuclear phagocyte lineage initially contain granules; these are lost during differentiation. The mononuclear phagocytes, which comprise from two to eight percent of the circulating leukocytes, contain enzymes similar to those present in neutrophils (Table 3.1). The enzymes are contained within bags bounded by membranes, called lysosomes. The mononuclear phagocyte is long-lived and continues to synthesize enzymes throughout its life. The acid hydrolases of mononuclear phagocytes act at acidic pH and cleave phosphate ester bonds that occur in proteins, polysaccharides, lipids, and nucleic acids. The enzymes are distinguished by their substrates and include fucosidase, 5′nucleotidase, galactosidase, arylsulfatase, mannosidase, N-acetyl-glucosaminidase, glucuronidase, and glycerophosphatase. Other enzymes included in this group are responsible for protein hydrolysis and are called cathepsins A, B, and C, and so on. Neutral proteases include cathepsin G, whose substrates are cartilage, proteoglycans, fibro-gen, and casein, and the enzymes, eiastase and collagenase. The latter two enzymes have been shown to play an important role in the destruction of normal tissues that may occur during an inflammatory response. The peroxidase enzyme catalase protects the phagocytes from the toxic effects of the hydrogen peroxide produced following the binding and phagocytosis of foreign substances.
Summation of Basic Endocrine Data
Published in George H. Gass, Harold M. Kaplan, Handbook of Endocrinology, 2020
Gastrin secretion is regulated by food in the stomach and small intestine. Mechanical wall distention activates stretch receptors, which in turn increase motility and secretion. The chemical stimuli are chiefly the peptides of protein hydrolysis. These act on the G cells and release gastrin in the very active or second (gastric) phase of stomach digestion. Stimulation of the vagal nerve fibers also helps to release gastrin.
Microencapsulation of β-carotene using barley residue proteins from beer waste as coating material
Published in Journal of Microencapsulation, 2023
Ana Cristina Freitas De Oliveira Meira, Larissa Carolina De Morais, Jayne De Abreu Figueiredo, Lizzy Ayra Alcântara Veríssimo, Diego Alvarenga Botrel, Jaime Vilela De Resende
Protein extraction from barley residue (BRP) was performed by subjecting the wet barley residue (64.47 ± 1.10% moisture content) to an alkaline extraction followed by isoelectric precipitation of the proteins, reaching a yield and protein content of 86.06 ± 5.86% and 20.41 ± 0.82%, respectively. Houde et al. (2018), when using this extraction method in defatted barley flour, obtained lower yield (51.4%) but higher protein content (68.9%). The discrepancies between the studies may be attributed to the difference between raw materials, since the barley residue is germinated barley grains that went through a mashing process. In this unit operation, enzymes act by promoting the degradation of starch into fermentable sugars and the hydrolysis of malt proteins by endoproteases (Yu et al.2020). Thus, the greater the removal of starch, the greater protein recovery yields are achieved (Houde et al.2018). On the other hand, protein hydrolysis contributes to the enrichment of the wort with proteins, reducing the content of this macromolecule in the residue.
Nano-liposomal zein hydrolysate for improved apoptotic activity and therapeutic index in lung cancer treatment
Published in Drug Delivery, 2022
Sahand Mazloum-Ravasan, Maryam Mohammadi, Elaheh Madadi Hiagh, Alireza Ebrahimi, Joo-Hyun Hong, Hamed Hamishehkar, Ki Hyun Kim
Zein is obtained as a by-product of corn starch processing and so that 45-50% of corn protein is composed of it. Due to the negative nitrogen balance and poor solubility in water, zein isolate is not directly applicable for human consumption (Shukla & Cheryan, 2001). Also, zein is widely used in nano drug delivery systems due to its good biocompatibility (Yu et al., 2020). Protein hydrolysis improves the function of a protein by modifying the protein, which involves chemical and biological changes that alter the physicochemical and functional properties of the protein by changing the structure of the protein (Yalcin & Çelik, 2007). Zein hydrolysate (ZH) has been shown to possess many beneficial effects, including antihypertensive (Miyoshi et al., 1991), anti-inflammatory (Liang et al., 2018), and antioxidant (Tang et al., 2010) effects, and it can relieve or reduce the risk of many chronic diseases (Ashaolu, 2020).
Cerebrospinal fluid proteomics reveal potential protein targets of JiaWeiSiNiSan in preventing chronic psychological stress damage
Published in Pharmaceutical Biology, 2021
Han-Zhang Wang, Wu-Long Luo, Ning-Xi Zeng, Hui-Zhen Li, Ling Li, Can Yan, Li-Li Wu
UBA1 is an essential and highly conserved protein in eukaryotes, encoded by the UBE1 gene (Xp11.3) on the Human X chromosome (Handley-Gearhart et al. 1994; Lv et al. 2018). Our proteomics results showed that Uba1 expression was decreased under CUMS and JWSNS restored the activity of Uba1 in the cerebrospinal fluid of stress-injured rats. Uba1 is a major E1 ubiquitin activase in mammalian cells and plays a role at the top of ubiquitin activation and conjugated cascade. It controls not only protein hydrolysis but also the cell cycle process, DNA damage repair, transcription, translation, vesicle transport and apoptosis. In the nervous system, UBA1 activity and ubiquitination are more broadly involved in the regulation of many aspects of neural function, such as neuronal differentiation, growth and development, neuronal excitability, neurotransmission, long-term enhancement (LTP), and synaptic formation and elimination (Mabb and Ehlers 2010; Kawabe and Brose 2011). Uba1 damage could lead to neuronal dysfunction and degeneration.