Improvement of functional properties and antioxidant activities of cuttlefish (Sepia officinalis) muscle proteins hydrolyzed by Bacillus mojavensis A21 proteases

Hmidet, Noomen; Balti, Rafik; Nasri, Rim; Sila, Assaâd; Bougatef, Ali

doi:10.1016/j.foodres.2011.05.023

Cited by 34 publications

(30 citation statements)

References 58 publications

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“…Highest foaming capacity (211 %) was observed for pepsin hydrolysate at pH 10.0. The pH of the dispersing medium significantly influences foaming properties, especially foam stability (Hmidet et al 2011). The results are in line with previous findings of foaming properties of protein hydrolysates prepared from cuttlefish (Sepia officinalis) muscle (Hmidet et al 2011).…”

Section: Foaming Propertiessupporting

confidence: 89%

“…The pH of the dispersing medium significantly influences foaming properties, especially foam stability (Hmidet et al 2011). The results are in line with previous findings of foaming properties of protein hydrolysates prepared from cuttlefish (Sepia officinalis) muscle (Hmidet et al 2011). Pepsin hydrolysate showed superior foam stability than undigested roe proteins, while trypsin hydrolysate exhibited lower foam stability than roe proteins.…”

Section: Foaming Propertiessupporting

confidence: 87%

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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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Section: Foaming Propertiessupporting

confidence: 89%

Section: Foaming Propertiessupporting

confidence: 87%

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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“…Haddar et al, 2009 [13] [14] had purified three detergent stable alkaline serine-proteases from the culture supernatant of B. mojavensis A21. Otherwise, B. mojavensis A21 proteases were used to produce hydrolysates of various proteins [15]- [17]. Haddar et al [18] optimized for B. mojavensis A21 culture conditions, by Plackett-Burman and Central Composite Design and the protease production was enhanced by 14 folds on hulled grain of wheat and sardinella peptone based medium.…”

Section: Introductionmentioning

confidence: 99%

Optimization of Protease Production by Bacillus mojavensis A21 on Chickpea and Faba Bean

Mhamdi¹,

Haddar²,

Mnif³

et al. 2014

ABB

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Response surface methodology (RSM) was employed to optimize the medium composition and culture conditions for the production of alkaline proteases by Bacillus mojavensis A21 on uncommon substrates: chickpea (CF) and faba bean (FF) flours. A significant positive influence of temperature, CF, FF, incubation time and inoculums size on the protease production was evaluated by Plackett Burman Design. Among these, CF was the most influential factor. The enhancement of protease to 9127 U/ml was achieved with the optimization procedure on the medium composed of (g/l): CF, 40; FF 30, NaCl 2.0; KH 2 PO 4 1; K 2 HPO 4 1; CaCl 2 , 0.1; MgSO 4 0.1. The cultures were conducted for 72 hours with an IS of 2%, at 30˚C, an agitation speed of 150 rpm and an initial pH of 8.0. More interestingly, the optimization was accomplished using two cheap and local fermentation substrates, CF and FF, which could result in a significant reduction in the cost of medium constituents. The maximum alkaline protease production was 9127 U/ml after 72 h of incubation and showed 5-fold increase in protease production over the initial level.

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“…The use of enzyme technologies for protein recovery and modification from food wastes and marine by-products is widespread, which has led to the production of a broad spectrum of novel food ingredients with improved functionalities [11,12] and various biological activities such as antioxidant activity [12,13], anticancer activity [14], antihypertensive activity [15], and antimicrobial activity [16]. In this field, our previous studies have successfully obtained protein hydrolysates from abalone (Haliotis discus hannai Ino) viscera and sea urchin (Strongylocentrotus nudus) gonads, which exhibited good antioxidant activities [17,18].…”

Section: Introductionmentioning

confidence: 99%

Functional properties of gelation-like protein hydrolysates from scallop (Patinopecten yessoensis) male gonad

Jin

Zhu

et al. 2012

Eur Food Res Technol

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Gelation-like protein hydrolysates from scallop (Patinopecten yessoensis) male gonad (SMG) were obtained by enzymatic hydrolysis using neutrase. Functional properties of SMG hydrolysates (SMGHs) with different degree of hydrolysis (DH: 4.94, 6.84, 7.53 and 11.86%, respectively) were evaluated with the objective to investigate the relations between hydrolysis characteristics and functionalities. The results showed that hydrolysis with neutrase improved the gelation property, solubility, waterholding capacity (WHC), oil-holding capacity (OHC), and surface hydrophobicity (SH), but not foaming capacity (FC) of SMG. The SMGHs at high DH (11.86%) showed better gelation property and solubility than that at low DH (4.94-7.53%). However, the maximum values of WHC, OHC, and SH of SMGHs were found at DH of 4.94%, significantly higher than (p \ 0.05) or equivalent to (p [ 0.05) that of soy protein isolate (SPI) for WHC and OHC. Emulsifying capacity of SMGHs is independent of DH, but restricted by pH environment. The emulsifying activity index of all SMGHs was significantly higher than that of SPI in pH 5 (p \ 0.05) and slightly higher than or equivalent to that of SPI in pH 7. Meanwhile, SMG and SMGHs were abundant in glycine, lysine, alanine, glutamic acid, and aspartic acid, containing all the essential amino acids (41.63-42.90% of the total amino acids). These results imply that SMGHs might be utilized as multifunctional and nutritive ingredients in food industry.

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Improvement of functional properties and antioxidant activities of cuttlefish (Sepia officinalis) muscle proteins hydrolyzed by Bacillus mojavensis A21 proteases

Cited by 34 publications

References 58 publications

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

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

Optimization of Protease Production by Bacillus mojavensis A21 on Chickpea and Faba Bean

Functional properties of gelation-like protein hydrolysates from scallop (Patinopecten yessoensis) male gonad

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