17E-10 |
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A. MORA-GUTIERREZ, A. J. Simmonds, and E. Risch. Cooperative Agricultural Research Center, Prairie View A&M University, Prairie View, TX 77446 Hydrolysis of casein by trypsin leads to the production of caseinophosphopeptides (CPP). CPP bind calcium ions and enhance the bioavailability of calcium, therefore, are valuable food additives. Bovine and caprine CPP differ in the casein ratio (as1- to as2-casein in particular) which may lead to different quality of surimi gels. Calcium compounds are used in pollock surimi as gel enhancers. Our objective was to investigate functions of calcium bound to bovine and caprine CPP in gel formation of Alaska pollock. Commercial surimi samples from Alaska pollock were used in this study. Pollock surimi was mixed with CPP, CaCl2, salt and water. For gel preparation, 0.2% CaCl2, 2% NaCl, and 78% moisture content were maintained. Two different levels of CPP (0, 0.5%) were added to the surimi paste. Surimi-CPP paste was cooked in cellulose casings in a 90oC water bath for 60 min. Textural properties of surimi gels were measured using standard techniques. Hardness, cohesiveness, and springiness were measured. The pollock surimi gel types tested showed measurable textural changes due to the kind and origin of the peptides. Bovine CPP in pollock surimi improved gel strength (10.42 N). Pollock surimi-bovine CPP gels also exhibited increased cohesiveness (0.84) and springiness (103.7 KPa). Pollock surimi-caprine CPP gels characterized by a low as1-casein content were of lesser strength than those of surimi-caprine CPP gels characterized by a high as1-casein content (9.25 and 9.87 N, respectively). In general, addition of bovine CPP resulted in surimi gels with the greatest strength (compressive and penetration forces), followed by caprine casein high in as1-casein and caprine casein low in as1-casein. CPP ¢richer¢ in as1-casein seem to produce acceptable pollock surimi gels and would accordingly deliver health benefit to consumers.
Session 17E, Food Chemistry: Proteins
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