Effects of ultrasound assisted extraction on the physiochemical, structural and functional characteristics of duck liver protein isolate

Zou, Ye; Wang, Li; Li, Pengpeng; Panpan, Cai; Zhang, Muhan; Sun, Zhilan; Sun, Chong; Zhong, Geng; Xu, Weimin; Xu, Xinglian; Wang, Daoying

doi:10.1016/j.procbio.2016.09.027

Cited by 74 publications

(59 citation statements)

References 55 publications

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“…It was observed that ultrasound treatment caused increase in the intensity of the peak at 757/cm, inferring that ultrasound increased the non-polar or hydrophobic nature of UPLPI. The result was similar to that of duck liver protein, in which the surface negative charge and hydrophobicity increased by 31.1% and 47.7% after ultrasound treatment, respectively (Zou et al 2017). Further, the effects of electrostatic repulsion were also enhanced correspondingly (Liu et al 2011) and the disulfide bonds changed (Jin et al 2015).…”

Section: Ftir Spectroscopysupporting

confidence: 75%

“…The peak positions had changed slightly after ultrasound treatment, and the evident peak shift of amide I band from 1633.9 to 1632.9/cm indicated that ultrasound could interact with the C=O of the polypeptide chain of the isolate and the hydrogen bond may be unfolded (Zou et al 2017). The result was similar to that of duck liver protein, in which the surface negative charge and hydrophobicity increased by 31.1% and 47.7% after ultrasound treatment, respectively (Zou et al 2017). In respect to amide II band, the peak positions had moved from 1524.5 to 1523.0/cm.…”

Section: Ftir Spectroscopymentioning

confidence: 99%

“…The FTIR spectra in Figure 2 of PLPI and UPLPI showed two strong absorption bands at amide I and II peaks. The peak positions had changed slightly after ultrasound treatment, and the evident peak shift of amide I band from 1633.9 to 1632.9/cm indicated that ultrasound could interact with the C=O of the polypeptide chain of the isolate and the hydrogen bond may be unfolded (Zou et al 2017). An increase in wave number revealed that part of a-helix or random coil in UPLPI had turned into b-sheet.…”

Section: Ftir Spectroscopymentioning

confidence: 99%

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Optimization and physicochemical properties of nutritional protein isolate from pork liver with ultrasound‐assisted alkaline extraction

Zou

Bian

et al. 2017

Animal Science Journal

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The aim of this study was to investigate the optimal conditions of ultrasound-assisted alkaline extraction (UAAE) on pork liver protein isolate (UPLPI) and its physico-chemical properties. Response surface methodology was used to determine the optimal conditions for UAAE, which were at ultrasonic power 265 W, ultrasonic time 42 min, NaOH concentration 0.80%, temperature 50°C, and solvent/raw material ratio 70. The extraction yield and efficiency of UPLPI were significantly improved over the conventional alkaline extraction (PLPI). The results of amino acid composition showed that UAAE could increase serine (36.5 g/kg), arginine (38.1 g/kg), alanine (37.5 g/kg), proline (48.7 g/kg), phenylalanine (55.6 g/kg) and lysine (47.2 g/kg) elution amount. The changes in fourier transform infrared spectra indicated unfolding and destruction of the protein structure in UPLPI. The differential scanning calorimetry analysis presented UPLPI with a slightly lower onset and peak denaturation temperature over PLPI. Surface hydrophobicity increased and the microstructures presented larger and more pores of UPLPI, therefore, it had better in vitro digestibility than PLPI. Therefore, UPLPI might have a potential application prospect in the food field due to its changes on molecular structure as well as on the microstructure of protein by UAAE.

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Section: Ftir Spectroscopysupporting

confidence: 75%

Section: Ftir Spectroscopymentioning

confidence: 99%

Section: Ftir Spectroscopymentioning

confidence: 99%

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Optimization and physicochemical properties of nutritional protein isolate from pork liver with ultrasound‐assisted alkaline extraction

Zou

Bian

et al. 2017

Animal Science Journal

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“…The majority of protein isolates and concentrates applied in the food industry are derived from plants, such as wheat, soybeans, sesame, and legumes (Chen, Chen, Ren, & Zhao, ; Matsumiya & Murray, ). There are also some animal protein isolates from chicken, pork, and beef (Darine, Christophe, & Gholamreza, ; Zou et al., ). However, due to dietary preferences and territory restrictions, consumers and food manufacturers are seeking replaceable aquatic protein sources for the human diet.…”

Section: Introductionmentioning

confidence: 99%

Physiochemical Properties and Functional Characteristics of Protein Isolates from the Scallop (Patinopecten yessoensis) Gonad

Han

Tang

et al. 2019

Journal of Food Science

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Protein isolates were recovered from scallop (Patinopecten yessoensis) gonads to develop a novel functional matrix by investigating their physiochemical and functional properties. Scallop gonad protein isolates (SGPIs) were prepared from degreased scallop gonads (DSGs) by an alkali extraction and isoelectric solubilization/precipitation (ISP) process. The protein compositions of the SGPIs were mainly vitellogenin and beta-actin with molecular weights of 266 and 42 kDa, respectively, as determined using Nano-liquid chromatography-mass/mass (Nano-LC-MS/MS). After the ISP process, the protein solubility of the SGPIs was significantly improved, and the surface hydrophobicity of SGPIs intensely increased by 1.1-fold, which were attributed to the exposure of aromatic residues such as phenylalanine, tyrosine, and tryptophan. However, the content of total/reactive sulfhydryl in SGPIs was decreased compared with that of DSGs. Meanwhile, the ISP process caused partial protein unfolding, as indicated by circular dichroism analysis, which exhibited a remarkable rise in the β-sheet content with a parallel decline in the α-helix and random coil contents (P < 0.05). SGPIs exhibited a better oil absorption capacity and foaming property than both DSGs and soybean protein isolates (SPIs). Moreover, the emulsifying capacity of SGPIs was greatly enhanced by the ISP process, which was superior to the effect of commercial SPIs and was ascribed to its favorable solubility as well as surface characteristics.Practical Application: During the processing of scallop (Patinopecten yessoensis) adductors, scallop gonad, a high-protein part, is usually discarded as processing by-products despite its edibility. In recent years, scallop gonads are regarded as good sources to develop protein matrices due to their high protein content and numerous nutrients. In this study, scallop gonad protein isolates (SGPIs) were isolated by isoelectric solubilization/precipitation (ISP) process. The preferable solubility, foaming property coupled with high emulsifying property of SGPIs indicated that the SGPIs could be potentially utilized as a good protein emulsifier and additives in production of kamaboko gels, hamburger patties, sausages, and pet foods. Further reproduction without permission is prohibited Food ChemistryPhysiochemical and functionalities of scallop protein . . . Protein in-gel digestionAccording to the protocol described by Qin and Zhang (2002), after conventional SDS-PAGE, the protein bands from the gel were excised, diced into small pieces (1 mm 3 ), and then dehydrated with 100 mMNH 4 HCO 3 /50% acetonitrile (ACN). Afterward, the gel pieces were reduced by dithiothreitol (DTT) solution, followed by alkylation using iodoacetamide/NH 4 HCO 3 solution, and then

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“…Duck meat and its products are highly appreciated by customers worldwide (Kim et al 2016). Moreover, duck meat and its products have gained increased consumer interest since it is recommended to reduce the intake of red meat, which has been related to cardiovascular disease (Adzitey et al 2012;Witak, 2008;Zou et al 2017b). The consumption of duck meat and its products has increased about twofold in China between 2000 and 2011 (Wang et al 2013;Wang et al 2016;Wang et al 2014).…”

Section: Introductionmentioning

confidence: 99%

Optimization of Flavourzyme Hydrolysis Condition for the Preparation of Antioxidant Peptides from Duck Meat using Response Surface Methodology

et al. 2018

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The aim of this study was to optimize and characterize Flavourzyme hydrolysis conditions for the preparation of antioxidant peptides from duck meat, using response surface methodology. The results indicated that optimal Flavourzyme hydrolysis conditions for preparation of antioxidant peptides from duck protein were a temperature of 50.19 °C, pH 5.45, and a reaction time of 1.03 h. Compared to non-hydrolyzed duck meat, Flavourzyme hydrolysis significantly improved the hydroxyl-radical scavenging, DPPH radical-scavenging, ferrous ion-chelating, reducing, and ABTS radical cation-scavenging activities of duck meat. Therefore, Flavourzyme can be regarded as an effective hydrolytic enzyme for the preparation of antioxidant peptides from duck meat.

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Effects of ultrasound assisted extraction on the physiochemical, structural and functional characteristics of duck liver protein isolate

Cited by 74 publications

References 55 publications

Optimization and physicochemical properties of nutritional protein isolate from pork liver with ultrasound‐assisted alkaline extraction

Optimization and physicochemical properties of nutritional protein isolate from pork liver with ultrasound‐assisted alkaline extraction

Physiochemical Properties and Functional Characteristics of Protein Isolates from the Scallop (Patinopecten yessoensis) Gonad

Optimization of Flavourzyme Hydrolysis Condition for the Preparation of Antioxidant Peptides from Duck Meat using Response Surface Methodology

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