Autolysis study of bigeye snapper ( Priacanthus macracanthus) skin and its effect on gelatin
Autolysis of bigeye snapper ( Priacanthus macracanthus) skin was studied. The maximal autolytic activity was observed at 60 °C and pH 7.5. The proteolytic activity was strongly inhibited by 0.001 mM soybean trypsin inhibitor (SBTI), whereas pepstatin A (1 μM), EDTA (20 mM), EGTA (10 mM), iodoacetic...
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Published in | Food hydrocolloids Vol. 21; no. 4; pp. 537 - 544 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford
Elsevier Ltd
01.06.2007
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | Autolysis of bigeye snapper (
Priacanthus macracanthus) skin was studied. The maximal autolytic activity was observed at 60
°C and pH 7.5. The proteolytic activity was strongly inhibited by 0.001
mM soybean trypsin inhibitor (SBTI), whereas pepstatin A (1
μM), EDTA (20
mM), EGTA (10
mM), iodoacetic acid (1
mM), PMSF (1
mM), E-64 (10
μM) and 1,10-phenanthroline (1
mM) showed no inhibitory effect. The result suggests that the major proteinase in bigeye snapper skin was a serine proteinase. Gelatin was extracted from bigeye snapper skin in water without and with 0.001
mM SBTI using a skin/water ratio of 1:7 at different temperatures (35, 40, 45, 50, 55 and 60
°C) for 12
h. In the presence of SBTI, the degradation was markedly inhibited. However,
β-chain disappeared and
α-chains underwent degradation to some extent at temperatures above 50
°C. Generally, a higher yield of gelatin was obtained as the extracting temperature increased (
P<0.05). Nevertheless, the addition of 0.001
mM SBTI caused a lower gelatin yield. Therefore, heat-activated serine proteinase, most likely collagenase, involved in the degradation of collagen molecule and affected the yield and proteinaceous components in the resulting gelatin from bigeye snapper skin. |
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Bibliography: | http://dx.doi.org/10.1016/j.foodhyd.2006.05.012 |
ISSN: | 0268-005X 1873-7137 |
DOI: | 10.1016/j.foodhyd.2006.05.012 |