Characterization of gelatin from bovine skin extracted using ultrasound subsequent to bromelain pretreatment

Ahmad, Tanvir; Ismail, Amin; Ahmad, Siti Aqlima; Khalil, Khalilah Abdul; Awad, Elmutaz Atta; Leo, Teik Kee; Imlan, Jurhamid Columbres; Sazili, Awis Qurni

doi:10.1016/j.foodhyd.2018.01.036

Cited by 38 publications

(30 citation statements)

References 63 publications

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“…The amino acid composition and MW distribution are two key factors that influence the properties of gelatin [ 20 ]. As shown in Table 1 , gelatin (STB-G) and Type I collagen (STB-C) from the bones of skipjack tuna had similar amino acid compositions.…”

Section: Resultsmentioning

confidence: 99%

Preparation and Characterization of Gelatin and Antioxidant Peptides from Gelatin Hydrolysate of Skipjack Tuna (Katsuwonus pelamis) Bone Stimulated by in vitro Gastrointestinal Digestion

et al. 2019

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In China, a large amount of fish bones are produced during the processing of tuna cans production. For full use of those by-products, gelatin (STB-G) with a yield of 6.37 ± 0.64% was extracted from skipjack tuna (Katsuwonus pelamis) bone using water at 60 °C for 8 h. Amino acid analysis showed that STB-G contained Gly (340.3 residues/1000 residues) as the major amino acid and its imino acid content was 177.3 residues/1000 residues. Amino acid composition, SDS-PAGE, and Fourier transform infrared (FTIR) spectrum investigations confirmed that the physicochemical properties of STB-G were similar to those of type I collagen from skipjack tuna bone (STB-C), but partial high molecular weight components of STB-G were degraded during the extraction process, which induced that the gelatin was easier to be hydrolyzed by protease than mammalian gelatins and was suitable for preparation of hydrolysate. Therefore, STB-G was hydrolyzed under in vitro gastrointestinal digestion (pepsin-trypsin system) and five antioxidant peptides were purified from the resulted hydrolysate (STB-GH) and identified as GPDGR, GADIVA, GAPGPQMV, AGPK, and GAEGFIF, respectively. Among the gelatin hydrolysate, fractions, and isolated peptides, GADIVA and GAEGFIF exhibited the strongest scavenging activities on 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (EC50 0.57 and 0.30 mg/mL), hydroxyl radical (EC50 0.25 and 0.32 mg/mL), superoxide anion radical (EC50 0.52 and 0.48 mg/mL), and 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical (EC50 0.41 and 0.21 mg/mL). Moreover, GADIVA and GAEGFIF showed a high inhibiting ability on lipid peroxidation in a linoleic acid model system. The strong activities of five isolated peptides profited by their small molecular sizes and the antioxidant amino acid residues in their sequences. These results suggested that five isolated peptides (STP1–STP5), especially GADIVA and GAEGFIF, might serve as potential antioxidants applied in health food industries.

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Section: Resultsmentioning

confidence: 99%

Preparation and Characterization of Gelatin and Antioxidant Peptides from Gelatin Hydrolysate of Skipjack Tuna (Katsuwonus pelamis) Bone Stimulated by in vitro Gastrointestinal Digestion

et al. 2019

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“…In addition, TG and TC were rich in alanine (Ala), proline (Pro), and hydroxyproline (Hyp) with a descending order. The amino acid pattern of gelatin (TG) was similar to those of gelatins from bovine heart [28] and skin [5], tuna bones and skin [4,24], and salmon, rohu and shark skins [24,29].…”

Section: Resultsmentioning

confidence: 99%

“…Furthermore, aromatic groups can stabilize radicals through donating protons to terminate the oxidative stress reaction [44,53]. Consequently, hydrophobic/aromatic amino acids, such as His, Pro, Met, Leu, and Phe, are regarded as the most important antioxidant factor of peptides [5,14]. For example, Jin et al reported that the high antioxidant activities of MCLDSCLL and HPLDSLCL were duo to the amino acid residues of Leu, Met, and His in their sequences [54].…”

Section: Resultsmentioning

confidence: 99%

“…According to the acid and alkali preparation processes, the produced gelatins were divided into type A and type B, with a molecular weight (MW) ranging from 80 to 250 kDa [3,4]. Moreover, acid or alkali with heating treatments led to the structure of gelatin being transited from helix to coli form and significantly increased the water solubility of gelatin [4,5]. Presently, more than 450 kilotons of gelatins are required to apply in food, nutraceuticals, beverage, pharmaceuticals, cosmetic, and photographic industries, and approximately 98.5% of the global commercial gelatins are extracted from mammalian species, such as pigs and cows [1,3,6].…”

Section: Introductionmentioning

confidence: 99%

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Gelatin and Antioxidant Peptides from Gelatin Hydrolysate of Skipjack Tuna (Katsuwonus pelamis) Scales: Preparation, Identification and Activity Evaluation

et al. 2019

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For full use of fish by-products, scale gelatin (TG) and antioxidant peptides (APs) of skipjack tuna (Katsuwonus pelamis) were prepared, and their properties were characterized using an amino acid analyzer, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Fourier transform infrared spectroscopy (FTIR), electrospray ionization mass spectrometers (ESI-MS), and radical scavenging assays. The results indicate that TG with a yield of 3.46 ± 0.27% contained Gly (327.9 ± 5.2 residues/1000 residues) as the major amino acid and its imino acid content was 196.1 residues/1000 residues. The structure of TG was more unstable than that of type I collagen from scales of skipjack tuna (TC) and TG was more suitable for preparation of hydrolysate by protease than mammalian gelatins. Therefore, TG was separately hydrolyzed under five proteases (pepsin, papain, trypsin, neutrase, and alcalase) and ten APs (TGP1–TGP10) were isolated from the alcalase-hydrolysate. Among them, TGP5, TGP7, and TGP9 with high antioxidant activity were identified as His-Gly-Pro-Hyp-Gly-Glu (TGP5), Asp-Gly-Pro-Lys-Gly-His (TGP7) and Met-Leu-Gly-Pro-Phe-Gly-Pro-Ser (TGP9), respectively. Furthermore, TGP5, TGP7, and TGP9 exhibited a high radical scavenging capability on 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (EC50 values of 1.34, 0.54, and 0.67 mg/mL, respectively), hydroxyl radical (EC50 values of 1.03, 0.41, and 0.74 mg/mL, respectively), and superoxide anion radical (EC50 values of 1.19, 0.71, and 1.59 mg/mL, respectively). These results suggest that three APs (TGP5, TGP7, and TGP9), especially TGP7, have a strong antioxidant activity and could act as potential antioxidant ingredients applied in functional products.

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“…Compared with the native gelatin, the peak of amide A band of the prepared GNPs shifts to a lower wavenumber with the increase of genipin dosage (8–12 wt%, the three kinds of particles are represented by the 8 wt% group, 10 wt% group, and 12 wt% group, respectively), indicating that N–H groups have participated in the formation of hydrogen bonds [37]. However, the 8 wt% group has the highest shift to low wavenumbers, which implied more hydrogen bonds formation than others.…”

Section: Resultsmentioning

confidence: 99%

Food-Grade Gelatin Nanoparticles: Preparation, Characterization, and Preliminary Application for Stabilizing Pickering Emulsions

Feng

Dai

et al. 2019

Foods

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In this paper, the food-grade gelatin nanoparticles (GNPs) were prepared by a two-step desolvation method and using genipin as a cross-linker. The GNPs with narrow size distribution and good dispersion could be obtained only at pH 12. The effect of the genipin dosage (8–12 wt%) on the GNPs was systematically investigated. The results showed that the cross-linking degree of the GNPs increased with the increasing dosage of genipin, thus leading to a more obvious cross-linking morphology observed from scanning electron microscope (SEM). The obtained GNPs showed a good dispersibility with a size range of 386–438 nm. However, the GNPs cross-linked by 8 wt% genipin dosage revealed a relatively higher size because of the aggregation induced by hydrogen bond. The 10 wt% group had good thermal stability and storage stability. The optical microscopy results showed that the Pickering emulsions (30–50 vol% internal phase) stabilized by the GNPs had good uniformity and stability, even after 30 days of storage time, suggesting that the stable GNPs had great potential in food-grade Pickering emulsions.

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Characterization of gelatin from bovine skin extracted using ultrasound subsequent to bromelain pretreatment

Cited by 38 publications

References 63 publications

Preparation and Characterization of Gelatin and Antioxidant Peptides from Gelatin Hydrolysate of Skipjack Tuna (Katsuwonus pelamis) Bone Stimulated by in vitro Gastrointestinal Digestion

Preparation and Characterization of Gelatin and Antioxidant Peptides from Gelatin Hydrolysate of Skipjack Tuna (Katsuwonus pelamis) Bone Stimulated by in vitro Gastrointestinal Digestion

Gelatin and Antioxidant Peptides from Gelatin Hydrolysate of Skipjack Tuna (Katsuwonus pelamis) Scales: Preparation, Identification and Activity Evaluation

Food-Grade Gelatin Nanoparticles: Preparation, Characterization, and Preliminary Application for Stabilizing Pickering Emulsions

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