Joe M. Regenstein

Growth, carcasss composition, and taste of rainbow trout of different strains fed diets containing primarily plant or animal protein

Abstract Ten rainbow trout (Salmo gairdneri) strains were evaluated during early growth from 30 g to 250 g on two diets — one based on plant protein (soybean and cottonseed meal) and the other on animal protein (fish meal). Diets were formulated to be nutritionally isocaloric and isonitrogenous. Fish were fed identical starter diets until they weighed 30 g. Significant differences in growth rate were found attributable to fish strain. Differences associated with diet were nonsignificant. Percent dress-out data based on eviscerated weight, deboned weight, and fillet weight also showed significant differences in yield attributable to fish strain, but not to diet. Carcass composition varied among strains, but none of the differences could be attributed to diet. Organoleptic tests showed no differences in flesh acceptability associated with either fish strain or diet, and all trout tested were equally acceptable to human taste panels.

Biochemical and physical changes of grass carp (Ctenopharyngodon idella) fillets stored at −3 and 0 °C

The objective of this study was to investigate the effect of superchilling at -3 °C compared with ice storage at 0 °C on the biochemical and physical properties of grass carp fillets. Fillets stored at -3 °C showed significant changes in whiteness, drip loss and textural hardness, while changes in pH, total volatile basic nitrogen and TCA-soluble peptides were slowed down. Partial denaturation of myosin as demonstrated by differential scanning calorimetry differed between fillets stored at -3 and 0 °C in that the transition peak showed a left shoulder at -3 °C and sharpened at 0 °C. Detachments between muscle cells and formation of cracks within cells were accelerated during storage at -3 °C, and from 10 days on, clear spaces between and within cells were observed with the concurrent appearance of white spots on the surface of fillets, suggesting the formation of both extra- and intracellular large ice crystals.

Collagen and Gelatin

Collagen and gelatin have been widely used in the food, pharmaceutical, and cosmetic industries due to their excellent biocompatibility, easy biodegradability, and weak antigenicity. Fish collagen and gelatin are of renewed interest, owing to the safety and religious concerns of their mammalian counterparts. The structure of collagen has been studied using various modern technologies, and interpretation of the raw data should be done with caution. The structure of collagen may vary with sources and seasons, which may affect its applications and optimal extraction conditions. Numerous studies have investigated the bioactivities and biological effects of collagen, gelatin, and their hydrolysis peptides, using both in vitro and in vivo assay models. In addition to their established nutritional value as a protein source, collagen and collagen-derived products may exert various potential biological activities on cells in the extracellular matrix through the corresponding food-derived peptides after ingestion, and this might justify their applications in dietary supplements and pharmaceutical preparations. Moreover, an increasing number of novel applications have been found for collagen and gelatin. Therefore, this review covers the current understanding of the structure, bioactivities, and biological effects of collagen, gelatin, and gelatin hydrolysates as well as their most recent applications.

Marine Bioactive Compounds and Their Health Benefits: A Review

The significance of marine creatures as a source of unique bioactive compounds is expanding. Marine organisms constitue nearly half of the wordwide biodiversity; thus, oceans and sea present a vast resource for new substances and it is considered the largest remaining reservoir of beneficial natural molecules that maight be used as functional constituents in the food sector. This review is an update to the information about recent functional seafood compounds (proteins, peptides, amino acids, fatty acids, sterols, polysaccharides, oligosaccharides, phenolic compounds, photosynthetic pigments, vitamins, and minerals) focusing on their potential use and health benefits.

Use of Hydrolysates from Yellowfin Tuna (Thunnus albacares) Heads as a Complex Nitrogen Source for Lactic Acid Bacteria

Two different peptones obtained by enzymatic hydrolysis of yellowfin tuna (Thunnus albacares) head waste have been shown to be effective in promoting the growth of lactic acid bacteria (Lactobacillus bulgaricus Persian Type Culture Collection (PTCC) 1332, Lactobacillus acidophilus PTCC 1643, Lactobacillus casei PTCC 1608, Lactobacillus delbrukii PTCC 1333, Lactobacillus plantarum PTCC 1058, Lactococcus lactis PTCC 1336, and Lactobacillus sakei PTCC 1712). Peptones obtained from the enzymatic hydrolysis with Alcalase or Protamex were used instead of the standard peptones used in commercial MRS media. Peptones produced by Alcalase and Protamex had a 34% and 19% degree of hydrolysis, respectively. The results showed that the peptones from Alcalase and Protamex were better at promoting lactic acid bacteria (LAB) growth than the commercial MRS media (P < 0.05). The choice of proteolytic enzyme used to produce the fish hydrolysate had a considerable impact on the performance of the resulting hydrolysate, both in terms of maximum growth rate and biomass production. Peptones produced using Alcalase, with a higher degree of hydrolysis, induced better growth and performed better overall as an LAB substrate than those using Protamex. Current study revealed that enzymatic-modified fish by-products can be used as low cast nitrogen source for bacterial growth.

SHELF-LIFE EXTENSION OF FRESH FISH — A REVIEW PART I — SPOILAGE OF FISH

In 1982 the world fish catch was 75 million tons live weight. About 70% (52 million tons) was used directly for human food (30% of which was consumed fresh). The catch provided 14% of the worlds need for animal protein, 4-5% of the total protein requirements, but less than 1 % of the nutritional energy needs (Whittle 1984). Fish is a good source of minerals such as calcium, phosphorous and iron, trace elements like iodine (in marine species), as well as vitamins. The high content of polyunsaturated fatty acids contributes significantly to the essential fatty acid requirements and, in addition, probably helps lower cholesterol levels. Thus, fish is important in the diet of the developing world. Within developing countries there is a recognizable trend for the poor to spend proportionally more of their household expenditure for animal protein on fish rather thmon other meat products (James 1984). By the year 2000 when the anticipated world population will be 6.1 billion people of which 90% will be living in developing countries, about 104 million tons of fish will be needed world-wide to meet the demand. There are three major ways to possibly meet this demand:

Antioxidant and antiproliferative activities of loach ( Misgurnus anguillicaudatus ) peptides prepared by papain digestion.

Loach protein hydrolysates (LPH) prepared by papain digestion were fractionated into four fractions, LPH-I (MW > 10 kDa), LPH-II (MW = 5-10 kDa), LPH-III (MW = 3-5 kDa), LPH-IV (MW < 3 kDa), and the in vitro antioxidant and antiproliferative (anticancer) activities of all fractions were determined. LPH-IV showed the lowest IC(50) value (16.9 ± 0.21 mg/mL) for hydroxyl radical scavenging activity and the highest oxygen radical scavenging capacity (ORAC) value (reaching 215 ± 5.9 mM Trolox/100 g loach peptide when the concentration was 60 μg/mL). Compared with other fractions, LPH-IV also exhibited stronger antiproliferative activity for human liver (HepG2), breast (MCF-7), and colon (Caco-2) cancer cell lines in a dose-dependent manner. When the protein concentration was 40 mg/mL, the HepG2 and MCF-7 cell proliferation of LPH-IV reached 7 and 4%, respectively, with no significant difference from those of LPH (8 and 7%, p > 0.05), with significantly less growth than those of LPH-I, LPH-II, and LPH-III, respectively (p < 0.05). The Caco-2 colon cell proliferation of LPH-IV was 12.8- and 8.7-fold smaller than those of LPH-I and LPH-II, respectively (p < 0.05). All of the fractions had a greater ability to inhibit Caco-2 colon cancer cell proliferation than to inhibit HepG2 liver cancer and MCF-7 breast cancer cell proliferation. The ORAC values of most of the fractions correlated (R(2) > 0.86, p < 0.01) with the antiproliferative activity of the three cancer cell lines, suggesting that higher antioxidant activity leads to better antiproliferative activity. However, further mechanistic and human clinical studies of the anticancer activity of loach protein hydrolysate fractions are needed.

Rheological properties of gelatin from silver carp skin compared to commercially available gelatins from different sources.

Gelatin is used as a functional ingredient in many foods, pharmaceuticals, and cosmetics as a stabilizing, thickening, and gelling agent. The rheological properties of gelatins are important in the potential functionality of gelatin. This study is designed to determine the rheological properties of gelatin extracted from the skins of silver carp (Hypophthalmichthys molitrix Valenciennes 1844). The extracted gelatin is compared with commercially available gelatins from different sources. The results indicate that the stress-strain relationship of gelatin gels remained in the linear region over a broad range of strains and stresses and gave similar elastic moduli at varying frequency, stress, and strain levels. One exception was a commercial high molecular weight fish skin gelatin that gave a lower elastic modulus indicating that its gel strength was low compared to the other gelatin samples studied. Gel strength varied between 220 and 1230 g while viscosity varied between 4.53 and 6.91 cP among the samples. Melting and gelling temperatures varied between 14.2 and 32.3 °C and 3.2 and 25.4 °C, respectively. Texture profile analysis was done at 2 deformation levels, 25% and 75%, and the results correlated well with gel strength. The correlations between hardness, cohesiveness, and gumminess and gel strength were 0.98, 0.82, and 0.99, respectively, at 25% deformation but lower at 75% deformation. The results suggest that rheological measurements might be used to quickly estimate gel strength using less material. In addition, the silver carp skin gelatin seemed to be of equal quality to some of the commercial gelatins.

The stoichiometry of the components of arthropod thin filaments

Limulus thin filaments confer calcium sensitivity on calcium-independent myosins and contain in addition to actin and tropomyosin, three troponin components. The molar ratio of actin:tropomyosin:troponin sub-unit T (TN-T): troponin sub-unit C (TN-C) is approximately 7:1:1:1, as in vertebrates, but twice the amount of the troponin sub-unit I (TN-I) may be present. Arthropod troponin binds approximately 1 mole Ca/mol troponin, a significantly smaller amount than bound by vertebrate troponin.

Chapter 5 - Fish Gelatin

Gelatin is a multifunctional ingredient used in foods, pharmaceuticals, cosmetics, and photographic films as a gelling agent, stabilizer, thickener, emulsifier, and film former. As a thermoreversible hydrocolloid with a narrower gap between its melting and gelling temperatures, both of which are below human body temperature, gelatin provides unique advantages over carbohydrate-based gelling agents. Gelatin is mostly produced from pig skin, and cattle hides and bones. Some alternative raw materials have recently gained attention from both researchers and the industry not just because they overcome religious concerns shared by Jews and Muslims but also because they provide, in some cases, technological advantages over mammalian gelatins. Fish skins from a number of fish species are among the other sources that have been comprehensively studied as sources for gelatin production. Fish skins have a significant potential for the production of high-quality gelatin with different melting and gelling temperatures over a much wider range than mammalian gelatins, yet still have a sufficiently high gel strength and viscosity. Gelatin quality is industrially determined by gel strength, viscosity, melting or gelling temperatures, the water content, and microbiological safety. For gelatin manufacturers, yield from a particular raw material is also important. Recent experimental studies have shown that these quality parameters vary greatly depending on the biochemical characteristics of the raw materials, the manufacturing processes applied, and the experimental settings used for quality control tests. In this review, the gelatin quality achieved from different fish species is reviewed along with the experimental procedures used to determine gelatin quality. In addition, the chemical structure of collagen and gelatin, the collagen-gelatin conversion, the gelation process, and the gelatin market are discussed.