Value added fish by-products - Nordic Innovation

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Frozen backbones were thawed overnight in a cold room, minced in a HOBART mincer (model AE 200). 2.1 Enzyme and chemicals Protamex TM (Novozymes A/S, Bagsvaerd, Denmark) was used for the hydrolysis. This enzyme was kindly delivered by Novozymes and complied with the recommend purity specifications for food-grade enzymes given by the Joint FAO/WHO Expert Committee on Food Additives (JECFA) and the Food Chemicals Codex (FCC) Anonymus 1998; Anonymus 2003. Protamex TM is shown as effective proteolytic enzyme in hydrolysis of cod backbones (Gildberg et al. 2002) and are commonly used in industrial application. A fish protein powder MariPep C ® , MariPep CK ® and MariPep P ® (all three were kindly submitted by Danish Fish Protein (Marinova aps.), Denmark), Norland hydrolysed fish collagen (HFC) (from Norland Products INC, Cranbury, USA) and fish protein powder (FPP) Aroma (from Aroma New Zealand Limited, New Zealand) were used as commercial available references. 2.2 Hydrolysis process 2.2.1 Hydrolysis process – fresh vs. frozen raw material The hydrolysis was performed in a 4 l closed glass vessel stirred with a marine impeller (150 rpm). Thawed (or fresh in part B) backbones were mixed with warm (55 o C) water at a weight ratio 1:1. When the temperature of the mixture was 55ºC, the enzymatic hydrolysis was started by adding 0.1% (by weight of raw material) Protamex TM . After different hydrolysis times: 10, 25, 45 and 60 min (A part) and 10 and 60 min (B part), enzyme inactivation was done by microwave heating for 5 min at a temperature higher than 90ºC. The bones were separated from the hydrolysate mixtures by sieving and the hot mixtures were centrifuged in 1L batches at 2250*g for 15 min. Two fractions were obtained after centrifugation: the sludge (non-water-soluble part) on the bottom and fish protein hydrolysate (FPH, water- soluble compounds). The fractions were separated by decanting. Both fractions were freeze- dried. The hydrolysis was performed in duplicate. 88
2.2.2 Hydrolysis process – Functional and antioxidative properties The hydrolysis was performed in a 4 l closed glass vessel stirred with a marine impeller (200 rpm). Minced backbones were mixed with warm (55 o C) water at a weight ratio 1:1. When the temperature of the mixture was 55ºC, the enzymatic hydrolysis was started by adding 0.1% (by weight of raw material) Protamex TM . After different hydrolysis times: 20 and 50 min enzyme inactivation was done by microwave heating for 5 min at a temperature higher than 90ºC. The bones were separated from the hydrolysate mixtures by sieving and the hot mixtures were centrifuged in 1L batches at 2250*g for 15 min. Two fractions were obtained after centrifugation: the sludge (non-water-soluble part) on the bottom and fish protein hydrolysate (FPH, water-soluble compounds). The fractions were separated by decanting. Both fractions were freeze-dried. The hydrolysis was performed in duplicate. 2.2.3 Hydrolysis process – FPH as antioxidants in model and food systems The hydrolysis was performed in a 4 l closed glass vessel stirred with a marine impeller (200 rpm). Minced backbones were mixed with warm (55 o C) water at a weight ratio 1:1. When the temperature of the mixture was 55ºC, the enzymatic hydrolysis was started by adding 0.2% (by weight of raw material) Protamex TM . After different hydrolysis times: 15,30 45,60, 120 and 130 min enzyme inactivation was done by microwave heating for 5 min at a temperature higher than 90ºC. The bones were separated from the hydrolysate mixtures by sieving and the hot mixtures were centrifuged in 1L batches at 2250*g for 30 min. Two fractions were obtained after centrifugation: the sludge (non-water-soluble part) on the bottom and fish protein hydrolysate (FPH, water-soluble compounds). The fractions were separated by decanting. FPH fractions were freeze-dried. The hydrolysis was performed in duplicate. 2.3 Functional, bioactive and antioxidative properties of hydrolysates obtained from cod (Gadus morhua) backbones 2.3.1 Chemical and functional properties 2.3.1.1 Chemical analyses Total nitrogen (N) was determined by CHN-S/N elemental analyser 1106 (Carlo Erba Instruments S.pA., Milan, Italy) and crude protein was estimated by multiplying total N by 6.25. These measurements were performed in triplicate. 89
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Maximum resource utilisation - Valu
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Title: Maximum resource utilisation
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mammalian gelatins. - Quantifying t
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• Extraction of gelatin from cold
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academia, both university and resea
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Sigurjon Arason, Magnea Karlsdottir
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3.3 Fish protein hydrolysate ......
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2.6.6 Emulsification properties and
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1 Introduction 1.1 Why this project
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1.2 Aim of the project The aim of t
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hydrophobicity, hydrophilicity, str
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minces of different fat content can
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Surimi is also used to make kosher
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capacity, by re-solubilisation of F
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Kristinsson & Rasco 2000a). In addi
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ioactive peptides. The activity is
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due to the strict EU regulations. T
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gelatin (326,000 tons), with pig sk
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3 Development and evaluation of ing
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Table 3.3. Organization of the resu
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Effects of bleeding, storage time,
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protein loss can be reduced with ra
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The results shows that from a produ
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Figure 3.4 Water holding capacity o
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3.2.3 Application of ingredients fr
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fillets into brine after injection
Page 53 and 54: Figure 3.7. Yield (%) of fresh cod
Page 55 and 56: Application of raw material and ing
Page 57 and 58: 3.3 Fish protein hydrolysate The wo
Page 59 and 60: Figure 3.11. Emulsifying capacity o
Page 61 and 62: Our work also shows that it is poss
Page 63 and 64: Sensory evaluation of lean fish pat
Page 65 and 66: Oxidation of the samples with added
Page 67 and 68: under harsher conditions. The stora
Page 69 and 70: effects on fish muscle, the gelatin
Page 71 and 72: epresents water (O-H stretching). T
Page 73 and 74: (Iceprotein), fish protein hydrolys
Page 75 and 76: Figure 3.18. Total yield 21 after c
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Page 79 and 80: and decreased water holding capacit
Page 81 and 82: Fish is a highly perishable raw mat
Page 83 and 84: 4.3 Next steps One of the main focu
Page 85 and 86: Figure 4.1. The project diagram. Th
Page 87 and 88: Bibliography Adler-Nissen, J. and O
Page 89 and 90: components: Evaluation of their ant
Page 91 and 92: Kristinsson, H. G., Theodore, A. E.
Page 93 and 94: Shahidi, F. (1994). Seafood process
Page 95 and 96: Appendix Materials and methods 79
Page 97 and 98: Table 1.1 Transverse relaxation tim
Page 99 and 100: Viscograph E enables automatic anal
Page 101 and 102: AOAC 937.18 (2000). Crude protein c
Page 103: scaling procedures of sensory attri
Page 107 and 108: (minced cod fillet, which were kept
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Page 111 and 112: amount of 16 amino acids was estima
Page 113 and 114: [O2], µM 250 200 150 100 50 0 [A]
Page 115 and 116: Table 2.1. Ingredients for fish cak
Page 117 and 118: 2.6.5.2 Fat absorption The absorpti
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Page 121 and 122: 3.1.7 Water activity (aw) The water
Page 123 and 124: 4.2 Comparison of the effect of inj
Page 125 and 126: 4.2.2.1.3 Boiling For the boiling p
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