Surface hydrophobicity and functional properties of myofibrillar proteins of mantle from frozen-stored squid (Illex argentinus) caught either jigging machine or trawling

Mignino, Lorena A.; Crupkin, Marcos; Paredi, María E.

doi:10.1016/j.lwt.2007.05.006

Cited by 28 publications

(21 citation statements)

References 32 publications

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“…Our results suggest that the components of 155 and 55 kDa could be products of degradation of MHC. Similar results were obtained with purified AM of mantle from frozen stored immature squid (I. argentinus) and in the AM of mantle and fin from frozen stored mature squid (Mignino et al, 2008;Mignino, Crupkin, & Paredi, 2011). As can be seen in Table 1 the relative percentages of M, PM, A, and myosin/actin (M/A) and myosin/ paramyosin (M/PM) ratios of AM from the mantle stored at 2-4°C.The AM stored in the absence of inhibitors shows a significant decrease (p < 0.05) in the percentage relative to myosin, the M/A and M/PM ratios at 24h of cold storage.…”

Section: Sds-polyacrylamide Electrophoresis (Sds-page)supporting

confidence: 84%

“…Emulsion of actomyosin solution of 2 mg/mL were formulate according to method previously described Mignino et al (2008). The EAI and ES were defined according to the method previously described (Xie & Hettiarachchy, 1997).…”

Section: Emulsifying Activity Index (Eai) and Emulsion Stability (Es)mentioning

confidence: 99%

“…observed a decrease in the MHC and the occurrence of component of 155-160 kDa in SDS-PAGE pattern of AM from mantle of frozen stored immature squid, which was attribute to proteolytic activity. For the same species during frozen storage at -30°C, was reported that the degradation of AM of the mantle is influenced by the method of capture used (Mignino, Crupkin, & Paredi, 2008). The presence of proteolytic activity in the mantle of other squid species has also been informed (Ebina, Nagashima, Ishizaki, & Takeshi,.…”

Section: Introductionmentioning

confidence: 97%

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Proteolytic Activity in Actomyosinfrom Mantle and Fin of Squid (Illexargentinus) Stored at 2-4°C. Influence on the Physicochemical and Functional Properties of the Protein

Mignino¹,

Crupkin²,

Paredi³

2013

JFR

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Actomyosin (AM) of mantle and fin from squid was stored at 2-4°C and the possible presence of proteolytic activity was investigated. Similar SDS-PAGE 10% patterns were obtained with both AM at zero time of storage. In absence of protease inhibitors, a decrease in the intensity of the band of the myosin heavy chain (MHC) and an increase in those of 155 kDa and 55 kDa bands of stored AM was observed. In presence of either PMSF (phenylmethylsulfonyl fluoride) or EDTA (ethylenediaminetetraacetic acid) both AM showed a minor degradation of the MHC, being the EDTA more effective. Proteolytic changes were accompanied by a significant increase (p < 0.05) in the proteinsurface hydrophobicity, (So: 1-anilino-8-naphtalene sulfonic acid (ANS)), the emulsion activity index (EAI) and the emulsion stability (ES) at 24 h of storage. At the same time, the reduced viscosity (VER) decreased significantly (p < 0.05). No significative changes (p > 0.05) in VER, IAE and ES of both AM occur in presence of protease inhibitors.A proteolytic activity closely associate with actomyosin from squid mantle and fin, was detected. Both serine and metalloproteinase activities were responsible for the autolysis of stored actomyosin. The best emulsifiying properties were obtained with AM without inhibitors. Because of this fins proteins could be and inexpensive source of functional ingredients with potential application as emulsifier agents in food product.

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Section: Sds-polyacrylamide Electrophoresis (Sds-page)supporting

confidence: 84%

Section: Emulsifying Activity Index (Eai) and Emulsion Stability (Es)mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

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Proteolytic Activity in Actomyosinfrom Mantle and Fin of Squid (Illexargentinus) Stored at 2-4°C. Influence on the Physicochemical and Functional Properties of the Protein

Mignino¹,

Crupkin²,

Paredi³

2013

JFR

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“…The particles around of 200 kDa can come from microorganism's membrane (More et al, 2014), the units of molecular weight around 110 and 66 kDa are related with sub units of αβ-heterodimers of some nitrobacterium (Spieck, 1996). The fractions from 21 to 36 kDa were grouped like tropomyosin, myosin related with muscular protein (Mignino et al, 2008), probably from feed and shrimp carcass. It is also necessary to consider, that the presence of small particles are related with process of freeze-dried (Spieck, 1996).…”

Section: Molecular Weight Distributionmentioning

confidence: 99%

“…References of several studies on food protein structure function relationships have emphasized the importance of protein hydrophobicity for protein functional properties after different treatments and/or processes (Mignino et al, 2008).…”

Section: Protein Surface Hydrophobicitymentioning

confidence: 99%

Physical and chemical characteristics of lyophilized biofloc produced in whiteleg shrimp cultures with different fishmeal inclusion into the diets

Arias‐Moscoso

Cuevas-Acuña

Rivas-Vega

et al. 2016

lajar

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ABSTRACT. Physical and chemical characteristics of lyophilized biofloc produced into the culture of whiteleg shrimp was determinated. The study consisted in the evaluation of biofloc produced with four experimental diets, isoproteic (35%) and isolipidic (8%), with different fishmeal content: 0 g kg -1 (T0), 100 g kg -1 (T1), 200 g kg -1 (T2), 300 g kg -1 (T3), and a commercial diet with 300 g kg -1 (TC) as a control. The shrimp was cultured in low salinity (5 g L -1) at a density of 600 ind m -3. The bioflocs were manually collected at day 28, lyophilized, and processed. Proximal composition was determined. To analyze morphology and particle size, photomicrographs were obtained using a Scanning Electron Microscope (SEM). Molecular weights of the protein hydrolysates were determined, and finally the bioflocs protein surface hydrophobicity (S0) was measured. No significant differences were detected for protein (360-404 g kg ) were different. The hydrolysate protein molecular weights were similar, in all cases varied from 22 to 200 kDa. The 50% of lyophilized particles had sizes from 3 to 15 μm. The fluorescence spectra slopes indicated differences in protein surface hydrophobicity (S0) between the treatments. In general, the physical and chemical characteristics of the bioflocs were independent of the used diet. The lyophilized biofloc has properties that allow its use as a protein source or raw material for biotechnological processes.

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Binding of aldehydes to myofibrillar proteins as affected by two‐step heat treatments

Wang

Zhao

et al. 2019

J Sci Food Agric

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BACKGROUND: The present study investigated the effect of two-step heat treatments on the structure of grass carp myofibrillar proteins (MPs) and their binding ability for selected aldehydes (hexanal, heptanal, octanal and nonanal). RESULTS: Within 30 min of the first heating step at 40 ∘ C and 5-10 min of the second heating step at 90 ∘ C, the enhancement of the flavor-binding ability was likely explained by the increases in surface hydrophobicity and total sulfhydryl content due to the unfolding of secondary structures of MPs through exposure of hydrophobic amino acids and sulfhydryl groups. Nevertheless, lengthy heating at 90 ∘ C accelerated the aggregation of unfolded MPs and reduced the hydrophobic bonding sites, thus weakening the hydrophobic interactions and decreasing the resultant binding ability of MPs with aldehydes.CONCLUSION: The binding ability of aldehydes to MPs was found to be strongly influenced by changes in protein structure and surface during the two-step heating process. The results provided insight into improving the flavor characteristics of freshwater fish surimi products.

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Surface hydrophobicity and functional properties of myofibrillar proteins of mantle from frozen-stored squid (Illex argentinus) caught either jigging machine or trawling

Cited by 28 publications

References 32 publications

Proteolytic Activity in Actomyosinfrom Mantle and Fin of Squid (Illexargentinus) Stored at 2-4°C. Influence on the Physicochemical and Functional Properties of the Protein

Proteolytic Activity in Actomyosinfrom Mantle and Fin of Squid (Illexargentinus) Stored at 2-4°C. Influence on the Physicochemical and Functional Properties of the Protein

Physical and chemical characteristics of lyophilized biofloc produced in whiteleg shrimp cultures with different fishmeal inclusion into the diets

Binding of aldehydes to myofibrillar proteins as affected by two‐step heat treatments

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