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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
The high concentration of hydrophobic amino acids may relate to the antihypertensive activity of collagen and gelatin and their hydrolysate peptides. Angiotensin-converting-enzyme (ACE) peptide inhibitors are naturally contained in various fish materials and marine collagen such as tuna (Hwang, 2010), Alaska pollack (Nakajima et al., 2009), salmon (Ohta et al., 1997), bonito (Fujita et al., 2000), shark (Wu et al., 2008), sardine (Otani et al., 2009), fish skin gelatin (Park et al., 2009), fish cartilage (Nagai et al., 2006) and squid tunic gelatin (Aleman et al., 2011). Peptides with high ACE inhibitory activity obtained from gelatin extract of Alaska pollack skin by serial hydrolysis using protease in the order alcalase, pronase E and collagenase (Byun and Kim, 2002). The high-ACE inhibitory activity was also exhibited by pepsin hydrolysate, which was obtained from Pacific cod skin gelatin using several enzymes (Ngo et al., 2016). Purified peptides from Thornback ray skin gelatin also showed ACE inhibitor activity (Lassoued et al., 2015).
Pharmaceutical Applications of Fenugreek Seed Gum
Published in Amit Kumar Nayak, Md Saquib Hasnain, Dilipkumar Pal, Natural Polymers for Pharmaceutical Applications, 2019
Dilipkumar Pal, Phool Chandra, Neetu Sachan, Md Saquib Hasnain, Amit Kumar Nayak
Fenugreek is known as Trigonella foenum-graecum belongs from the family Leguminosae is indigenous to the Mediterranean region, the northern part of Africa, the western part of Asia and Canada. The seeds of fenugreek have been employed in food and remedy as a component for many years (Brummer et al., 2003). Fenugreek seeds contain high percentages of carbohydrates, mainly polysaccharides. Fenugreek seed gum (FSG) is a soluble fiber obtained from the seeds of a legume plant, Trigonella foenum-graecum, which is commonly grown worldwide and predominantly in India. In a work, Brummer et al., (2003) extracted FSG as per the scheme depicted in Figure 9.1. Extraction procedure for fenugreek gum was found augmented in order to attain the low content of protein. Preliminary tests illustrated that during extraction, a lower temperature will yield the gums with less protein contaminants and significantly upsetting the yield. Therefore, a defatted, deactivated fenugreek seed produces FSG, which is optimized at 10°C for 2 h to provide a yield of 22% along with 2.36% protein contaminants (Table 9.1). Pronase was used to purify FSG, which further reduced protein contaminates to the level of 0.5% (Table 9.2) without upsetting the molecular weight of galactomannans. By HPSEC, changes in molecular weight were supervised.
Biodegradation Properties
Published in Chih-Chang Chu, J. Anthony von Fraunhofer, Howard P. Greisler, Wound Closure Biomaterials and Devices, 2018
In contrast, Williams and Mort151,152 demonstrated that certain enzymes, under some conditions, are able to influence the degradation of PGA and polylactides. Williams and Mort151 found that certain enzymes, under some in vitro conditions, were able to influence the degradation of 2/0 PGA sutures as shown in Table 7.17. Acid phosphates, papain, pepsin, peptidase, pronase, proteinase K, and trypsin had no apparent effect on PGA sutures. Ficin, carboxypeptidase A, chymotrypsin, and clostridiopeptidase A all produced significantly greater amounts of degradation, often increasing the rate of hydrolysis by a factor of two. Bromelain, esterase, and leucine amino peptidase-treated PGA sutures lost all of their tensile strength after 3 weeks, while the untreated ones lost only 13.3% of their original value within the same period. It was, however, difficult to take into account quantitatively the effect of ammonium sulfate whose presence in the media was required to stabilize the enzymes on the observed accelerated hydrolysis. The enzymes that did influence the hydrolysis were mainly (although not exclusively) of the type (esterases) that might be expected to attack an aliphatic polyester on the basis of its molecular structure.
Characterization and mode of action of a potent bio-preservative from food-grade Bacillus licheniformis MCC 2016
Published in Preparative Biochemistry and Biotechnology, 2019
Nithya Vadakedath, Prakash M. Halami
The activity of untreated ppABP against K. rhizophila ATCC 9341 was found to be 51200 AU mL−1. The ppABP was completely stable up to 100 °C for 15 min. However, the treatment of ppABP at 121 °C resulted in the reduction of its residual activity to 75% (Table S1). It also showed stability over a wide range of pH. No loss or reduction in activity of the ppABP against K. rhizophila ATCC 9341 was noted in any of the assayed pH conditions (pH 2–10). Like other bacteriocins of Bacillus (e.g. subtilosin A, cerein 8 A and thuricin 17, etc.), the ppABP of MCC 2016 was noted to be stable over a wide range of pH and temperature, indicating that it can be applied as a biopreservative in food systems with different pH and requiring high-temperature processing.[33,34] In the presence of proteolytic enzymes (proteinase K or trypsin), the ppABP lost its activity against K. rhizophila ATCC 9341 (Table S1). This indicates that the antibacterial compound produced by MCC 2016 is sensitive to proteolytic enzymes, therefore, suggesting that the antibacterial compound is proteinaceous in nature and could be used as a natural preservative in food with no harm to the consumers.[35] However, there are reports of the bacteriocins of Bacillus spp., e.g. cerein and coagulin I4, which are less resistant to proteolytic treatments.[31,34] Berić et al.[28] also reported that the antimicrobial activity of the bacteriocin licheniocin 50.2 from B. licheniformis VPS50.2 is insensitive to lysozyme and proteinase K, shows partial sensitivity to trypsin and is completely sensitive towards pronase E.
Optimization of primary freeze drying conditions for powdered chicken meat hydrolysate from mechanically deboned chicken residues
Published in Drying Technology, 2020
Chicken meat is a substantial food for consumers all over the world. It is rich in essential amino acids and involves large amount of proteins.[1] Increasing quantities of fresh deboned chicken meat and meat products are being produced and sold, so by-products such as chicken bones are increasingly generated during processing.[2] Meat by-products are very rich in proteins generally and thus, they comprise a good substrate for proteolysis.[3] Specific proteases like papain, bromelain, thermolysine, pronase or proteinase K are used for protein hydrolysis.[3] Protein hydrolysates are alternatives to consumers who is unable to digest whole/intact protein. In formulas, hydrolyzed proteins can be used for hyperallergic newborns because they also show reduced immunological reactivities. In addition, peptides may be an excellent source of nitrogen for sportmen/women, and peptides with high biological value are good alternatives as a protein supplement in extensive types of diets. Besides all of these area of use, protein hydrolysates are very instable because of their high protein and moisture content, and so they have to be processed to enhance their shelf lives. Spray drying method is most commonly used for drying protein hydrolysates obtained from different sources,[4–10] because spray drying method requires low operational costs and short processing times. But in terms of powder product quality, spray drying has some disadvantages including protein denaturation, changing the proportion and type of covalent or non-covalent interactions (and so, affecting the antioxidant activity of hydrolysates) and sticking to dryer chamber causing wall deposition.[11–16] Hence, freeze drying is highly suitable for reducing water activity by sublimation of water, minimizing enzymatic and microbiological reactions.[11] Freeze-drying (lyophilization) is a process in which the ice in a matrix sublimed into gas phase without melting. This process takes place in low temperatures and under high vacuum, because sublimation is only possible below the triple point of water.[17,18] The process has three stages: freezing, primary drying (sublimation) and secondary drying (desorption).[19–23] The most critical and longest step of the freeze-drying process is the primary drying stage. However, not only the freezing stage is important to determine the size, shape, and distribution of ice crystals (important for the final properties of the freeze-dried product), but also, freezing conditions (cooling rate, annealing treatments, and nucleation temperature) that causes the pores with different sizes generated during ice sublimation, can significantly affect the performance of drying process.[24–26]