FT-IR and Raman spectroscopies determine structural changes of tilapia fish protein isolate and surimi under different comminution conditions

Kobayashi, Yohnosuke; Mayer, Steven G.; Park, Jae W.

doi:10.1016/j.foodchem.2017.01.068

Cited by 119 publications

(62 citation statements)

References 38 publications

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“…-helical structure probably led to the exposure of active groups, which resulted in heat-induced chemical cross-linking and formed a three-dimensional network. 20 Previous studies 32,33 concerning other proteins have also indicated that a decrease in -helix content and an increase in -sheet content are general features in a translucent type of protein during heating and gelation, which is consistent with our study.…”

Section: Raman Spectrasupporting

confidence: 92%

Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Zhao

Wang

et al. 2019

J Sci Food Agric

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BACKGROUND The influence of heat‐induced structural modifications of grass carp myofibrillar protein (MP) on its ability to bind to selected aldehydes (hexanal, heptanal, octanal and nonanal) was investigated. The interactions of MP and flavor compounds were investigated using HS‐GC‐MS, intrinsic fluorescence spectra, Raman spectra, SDS‐PAGE, turbidity, total sulfhydryl content and surface hydrophobicity. RESULTS The ability to bind to aldehydes was strongly influenced by changes in the structure and surface of proteins during the heating process (0–30 min). During the first 0–10 min of heating, the flavor‐binding ability increased, which is likely attributable to increased surface hydrophobicity and total sulfhydryl content, and to the unfolding of secondary structures of MP by exposure to reactive amino acids, sulfhydryl groups and hydrophobic bonding sites. Nevertheless, lengthy heating (>10 min) caused protein refolding and accelerated aggregation of protein, thus reducing hydrophobic interactions and weakening the resultant capacity of MP to bind to flavor compounds. CONCLUSION The results suggested that hydrophobic interactions were enhanced upon short‐term heating, whereas long‐term heating weakend them. The results provide information concerning improvement of the flavor profile of freshwater fish surimi products. © 2019 Society of Chemical Industry

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Section: Raman Spectrasupporting

confidence: 92%

Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Zhao

Wang

et al. 2019

J Sci Food Agric

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“…Numerous voids with dark blue color, irregular shape and varied size (about 1 mm) were randomly distributed in all the pseudo-color images, related to the air bubbles formed during communition. 5 Regardless of comminution method, the pseudo-color images of gels became brighter as the comminution duration extended. Compared with blending, images were obviously brighter in the gels made by shearing, suggesting more immobilized and/or free water.…”

Section: Water Distributionmentioning

confidence: 99%

“…3,4 Investigation on gelling properties of surimi as influenced by comminution conditions including speed, final temperature, salting time, comminution time and vacuum, etc., have been reported. [5][6][7][8] During the comminution process, the increase of speed or duration led to the improvement on the heat-induced gelation of surimi paste, which was generally thought to be related with the increase of the solubilizing and unfolding of myofibrillar proteins. 1 However, as the duration was extended too long, gel strength gradually decreased which was mainly due to the partial aggregation of proteins before heating.…”

Section: Introductionmentioning

confidence: 99%

Gelling properties of silver carp surimi as affected by different comminution methods: blending and shearing

Liu

Shi

et al. 2019

J Sci Food Agric

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BACKGROUND Blending and shearing, two types of comminution methods, are widely used in the manufacturing of surimi‐based products. The comminution methods applied are varied to product types and manufacturers. In this study effects of different comminution methods (blending and shearing) on gelling properties of silver carp surimi were investigated. RESULTS Regardless of comminution methods, breaking force, penetration distance and water holding capacity of surimi gel significantly increased with comminution duration up to 10 min. As compared with blending, those values under shearing of the same duration were significantly higher. Within 3 min of comminuting whiteness values of gels by shearing were significantly higher than those by blending. Electrophoresis studies showed that comminution method had no obvious effect on protein patterns. Scanning electron microscopy images revealed that more uniform and denser network was formed in the surimi gels made by shearing. Water distribution of the gels made by shearing was obviously more uniform according to magnetic resonance imaging analysis. CONCLUSION Our results suggested that with respect to blending, shearing was a better choice to maximize the gelling ability of silver carp surimi, which resulted in the higher values of texture, whiteness and water holding capacity. It could be attributed to the denser three‐dimensional network and more uniform water distribution of the surimi gel prepared by shearing. © 2019 Society of Chemical Industry

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“…Surimi is a kind of stabilized myofibrillar proteins obtained from deboned fish mince, in which blood, lipids, sarcoplasmic proteins, and other impurities have been washed out with cold water (Alakhrash, Anyanwu, & Tahergorabi, ; Kobayashi, Mayer, & Park, ). Surimi can be made into surimi products of high price, such as fish ball, fish sausage, kamaboko, and crabstick, which are popular in China, Thailand, Malaysia, and other Southeast Asia countries (Campo & Tovar, ; Yin & Park, ).…”

Section: Introductionmentioning

confidence: 99%

The effect of modified starches on the gel properties and protein conformation of Nemipterus virgatus surimi

et al. 2019

Journal of Texture Studies

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The study investigated the effect of native cassava starch (NCS), hydroxypropylated starch, acetic acid esterification starch (AAES), acetylated distarch phosphate on gel properties and protein conformation of Nemipterus virgatus surimi. Addition of 10 g kg−1 NCS or 20 g kg−1 AAES could significantly promote the gel strength and textural profiles of the surimi gels (p < .05). The water holding ability and whiteness of surimi were remarkably increased when the four types of starch were added at all concentrations (p < .05). In rheological test, the lower G′ was observed in surimi samples added with starch at low temperature, suggesting starch played an inactive filler role in surimi. Along with the increase of starch additive amount, ionic bond and hydrophobic interaction first increased and then decreased, while hydrogen bond first decrease and then increased. According to Raman spectroscopy data, small content of starch promoted the heat‐induced conformational transition of surimi protein from α‐helix to β‐sheet, leading to the change in gel properties of surimi gels. Scanning electron microscopy photographs showed surimi gels added with 20 g kg−1 starch had the finer and denser network structure. Therefore, 20 g kg−1 AAES or 10 g kg−1 NCS or 10 g kg−1 HS could be proposed to a potential modifier to effectively improve the quality of surimi products.

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FT-IR and Raman spectroscopies determine structural changes of tilapia fish protein isolate and surimi under different comminution conditions

Cited by 119 publications

References 38 publications

Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Gelling properties of silver carp surimi as affected by different comminution methods: blending and shearing

The effect of modified starches on the gel properties and protein conformation of Nemipterus virgatus surimi

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