title: Control of lightness and firmness of cold and reheated frankfurter-type sausages using different spectroscopic methods applied to raw batter.
abstract: Muscle types and collagen, fat, and muscle protein minus collagen were varied in cooked frankfurter-type sausages made from beef and pork meat as well as pork backfat. The content of collagen was fixed at preset levels with pork rind. The amount of total muscle protein in the sausages varied between 5.9% and 11.9% and the fat between 16.1% and 22.1%. The collagen content varied between 1.3% and 4%. Spectroscopic measurements (near-infrared reflectance spectra 1100 to 2500 nm; front-face autofluorescence emission spectra 360 to 640 nm) on raw batters were used to predict the amounts of total muscle protein minus collagen, collagen, myoglobin, and fat (biochemical components), L* values from a Minolta chromameter, and firmness of cold (22 degrees C) and reheated sausages (60 degrees C). Lightness of sausages was most accurately determined from the batter data with a Minolta chromameter or the autofluorescence measurement system. Firmness of cold sausages could be described by the amounts of biochemical components plus the type of muscle used in the sausage. The 2nd-best approach was to use the shape of the near-infrared spectra to determine firmness. This was possible as the shape of near-infrared spectra depended on total protein content, and total protein content largely determined the firmness of cold sausages. If the sausages were reheated to 60 degrees C, near-infrared spectroscopy alone determined firmness of the sausages with a lower accuracy than a combined solution of fluorescence and near-infrared spectroscopy. The 2 spectroscopic techniques could thus be used to estimate the amount of biochemical components in sausages. Once these components were known, firmness could be calculated from a model between the amounts of biochemical components and firmness. For reheated sausages, as opposed to cold ones, there was a need to differentiate between collagen and the other muscle proteins in order to determine firmness. This was optimally achieved by using both autofluorescence and near-infrared spectroscopy.
authors.affiliation: Institute of Chemistry, Biotechnology and Food Science Univ. of Life Science, P.O. Box 5003, N-1432-As, Norway. bjorg.egelandsdal@umb.no
authors.forename: B
authors.initials: B
authors.lastname: Egelandsdal
authors.forename: G I
authors.initials: GI
authors.lastname: Dingstad
authors.forename: G
authors.initials: G
authors.lastname: Tøgersen
authors.forename: K I
authors.initials: KI
authors.lastname: Hildrum
mesh_terms: D000818:Animals; D002417:Cattle; D003094:Collagen / Q000032:analysis; D005227:Fatty Acids / Q000032:analysis*; D005504:Food Analysis / Q000379:methods; D006801:Humans; D008461:Meat Products / Q000032:analysis* / Q000592:standards*; D009124:Muscle Proteins / Q000032:analysis*; D009211:Myoglobin / Q000032:analysis; D012212:Rheology; D019265:Spectroscopy, Near-Infrared / Q000379:methods*; D013552:Swine
chemical_list: D005227:Fatty Acids; D009124:Muscle Proteins; D009211:Myoglobin; D003094:Collagen