Antioxidant and functional properties of protein hydrolysates from pink perch (Nemipterus japonicus) muscle

Naqash, Shabeena Yousuf; Nazeer, R. A.

doi:10.1007/s13197-011-0416-y

Cited by 78 publications

(62 citation statements)

References 25 publications

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“…Their IC 50 value was reported to be 2.1 ± 0.1 mg/mL respectively, which was comparable to that of protein hydrolysates obtained from Alaska pollak, sardine and sea bream (Naqash and Nazeer 2013). The existences of amino acids that are hydrophobic in nature are known to contribute to their ACE-inhibitory activity as they bind with the catalytic sites of ACE and inhibit them (Wijesekara and Kim 2010).…”

Section: Angiotensin-i-converting Enzyme Inhibitory Activitymentioning

confidence: 64%

Production and characterization of functional properties of protein hydrolysates from egg shell membranes by lactic acid bacteria fermentation

Jain

Anal

2017

J Food Sci Technol

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This study aimed to ferment the chicken eggshell membrane (ESM) using the lactic acid bacteria, Lactobacillus plantarum for preparation of functional and bioactive protein hydrolysates. Cultivation at an initial pH of 8.0 for 36 h resulted in maximum protein concentration (177.3 mg/g) and degree of hydrolysis (25.1%) of the hydrolysates. Fermentation resulted in the production of hydrolysates that demonstrated excellent solubility (90.7%), good foaming capacity (36.7%) and emulsification activity (94.6 m 2 /g). Additionally, these protein hydrolysates exhibited remarkable bioactive properties for instance reducing power (2.53), protection from DPPH radical (70.5%) and angiotensin I converting enzyme inhibition (49.3%). The fermented protein hydrolysates were also found effective against various foodborne pathogens. The protein hydrolysates obtained by fermentation of ESM can be potentially incorporated in functional foods and nutraceuticals resulting in valorization of the ESM waste.

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Section: Angiotensin-i-converting Enzyme Inhibitory Activitymentioning

confidence: 64%

Production and characterization of functional properties of protein hydrolysates from egg shell membranes by lactic acid bacteria fermentation

Jain

Anal

2017

J Food Sci Technol

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“…Proteolysis of food proteins might produce some peptides with antihypertensive or antioxidant activity, which could be served as functional food ingredients such as angiotensin I-converting enzyme (ACE) inhibitors (Ariyoshi 1993;Janitha et al 2002;Meisel 1997;Robert et al 2004;Yamamoto 1997) or antioxidants (Naqash and Nazeer 2011;Sun et al 2011). Milk proteins are particularly good sources of ACE-inhibitory peptides and had been widely studied in the past (da Costa et al 2007;López-Fandiño et al 2006;Miguel et al 2009;Ortiz-Chao et al 2009).…”

Section: Introductionmentioning

confidence: 99%

Optimization of some conditions of Neutrase-catalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase

Kong

Zhao

2011

J Food Sci Technol

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Casein hydrolysate was prepared by hydrolyzing casein with Neutrase and then modified by a Neutrasecatalyzed plastein reaction. The prepared hydrolysate had a degree of hydrolysis of 13.0% and exhibited ACE inhibition in vitro with an IC 50 value of 40.4 μg⋅mL −1 . With the decreased amount of free amino groups of the modified hydrolysate as the response, some conditions of the plastein reaction including substrate concentration, enzyme to substrate ratio, reaction temperature and time were studied by single factor experiments and response surface methodology, and optimized finally as 62% (w/w), 3.0 kU⋅g −1 peptides, 30°C and 6.3 h, respectively. The maximum decreased amount of free amino groups of the modified hydrolysate prepared under these optimized conditions was 210.0 μmol⋅g −1 peptides, while corresponding IC 50 value was lowered to 14.7 μg⋅mL −1 . The present result indicates that Neutrase-catalyzed plastein reaction was capable of enhancing ACE-inhibitory activity in vitro of casein hydrolysate, and also highlights the importance of a forthcoming study to investigate the peptide compositions of the modified hydrolysate and the role of protease used in the plastein reaction.

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“…As shown in the Fig. 3, the solubility of pepsin and trypsin hydrolysates from rohu roe proteins was higher than that obtained by the protein hydrolysates from pink perch muscle (Naqash and Nazeer 2013) and the protein hydrolysates prepared from Cirrhinus mrigala roe (Chalamaiah et al 2010) exhibited comparable solubility profiles. The present results clearly indicated that the enzymatic hydrolysis by pepsin and trypsin was an effective way to increase solubility of rohu roe proteins.…”

Section: Protein Solubilitymentioning

confidence: 79%

Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeo rohita) roe (egg) prepared by gastrointestinal proteases

et al. 2015

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Previously, we have reported the chemical composition, molecular mass distribution and antioxidant activity of rohu roe protein hydrolysates. In the current study, antiproliferative, angiotensin-converting enzyme (ACE)-inhibitory activities and functional properties of protein hydrolysates from rohu (Labeo rohita) roe proteins, prepared by gastrointestinal proteases (pepsin and trypsin), were investigated. Antiproliferative activity was evaluated against human colon cancer cell line Caco-2. The results showed that the pepsin hydrolysate possessed dose dependent inhibitory effect on Caco-2 cell line. Pepsin and trypsin hydrolysates displayed ACE-inhibitory activity in vitro. The ACE-inhibitory activity of the hydrolysate generated by pepsin (47 ± 1.7 %, at 1 mg/ml) is higher than that obtained by trypsin (36 ± 3.2 %). Additionally, the undigested rohu roe proteins and its hydrolysates exhibited functional properties. Solubilities of the hydrolysates were above 81 ± 9.2 % at all pH values tested. Pepsin and trypsin hydrolysates showed good foaming capacity (45-211 %) and emulsification activity (4-29 m 2 /g). The foaming abilities and emulsifying activity index (EAI) were affected by pH. The results suggest that protein hydrolysates from rohu roe could be useful in food industry for various applications.

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Antioxidant and functional properties of protein hydrolysates from pink perch (Nemipterus japonicus) muscle

Cited by 78 publications

References 25 publications

Production and characterization of functional properties of protein hydrolysates from egg shell membranes by lactic acid bacteria fermentation

Production and characterization of functional properties of protein hydrolysates from egg shell membranes by lactic acid bacteria fermentation

Optimization of some conditions of Neutrase-catalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase

Antiproliferative, ACE-inhibitory and functional properties of protein hydrolysates from rohu (Labeo rohita) roe (egg) prepared by gastrointestinal proteases

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