In-Line Estimation of Fat Marbling in Whole Beef Striploins (Longissimus lumborum) by NIR Hyperspectral Imaging. A Closer Look at the Role of Myoglobin

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Development of vibrational spectroscopic techniques for measuring quality-related parameters of connective tissue.

The aim of this work was to study by Fourier-transform infrared (FT-IR) micro spectroscopy different parameters of connective tissue, which have previously been related to meat tenderness. These parameters were collagen fiber orientations, collagen and sulfated glycosamineoglycans (GAGs) content, and their relative ratio during storage. Two different bovine muscles were studied, M. psoas major (PM) and M. Semitendinosus (ST). These muscles are known to differ in tenderness, with the PM muscle as the most tender. The muscles were aged at 4º for 19 days and samples were taken for spectroscopic, biochemical and histological analysis every third day. Mechanical measurements (Warner Bratzler) were done to confirm the textural properties in the two muscles. Biochemical measurement by DMB and histological staining by Alcian blue were used to verify the content and distribution of sulfated GAGs in the two muscles during aging. The tissue sections were also stained with collagen I antibodies to see the distribution of collagen in the connective tissue in the two muscles. The tissue section was measured by (FT-IR) micro spectroscopy using single spectra and polarized light microscopy imaging. The absorbance peaks obtained from single spectra were related to the connective tissue parameters, and the polarized measurement was used to investigate the direction of the collagen fibers in the connective tissue. The sulfate stretch band at 1237 cm-1 in the infrared spectrum showed a decrease in sulfated GAGs in both muscles during storage, in accordance with biochemical and histological results. The ST muscle had a higher content of sulfated GAGs and had a more pronounced decrease measured biochemically, and the same result were also obtained in the spectra. The collagen absorption band at 1659 cm-1showed a possible degradation of cross-links in the PM muscle, however, using a different cross-links ratio (1660:1690) no difference were found. The absorbance at 1654 cm-1 could indicate a conformation change in the collagen α- helix in the PM muscle. Two bands in the water region were assigned to hydrogenated and non-hydrogenated N-H starching bands at ~3290 and ~3335 cm-1 respectively. These water bands could be used to estimate the hydrogenation of connective tissue proteins and shows that the water content in the samples is decreasing during storage. The polarized measurements showed that the collagen fibers in the PM muscle had a random orientation, while fibers in the ST muscle showed an orientation parallel to the x- axis early in the period and a random orientation after 11 days post mortem storage. Staining with antibodies against collagen I supported these results, showing that the perimysium of PM had III a more diffuse staining pattern compared to the ST muscle which showed a more wavy appearance with clear thread-like like structures. Our results from this study show that FT-IR micro spectroscopy is promising in evaluating connective tissue in bovine skeletal muscles. Good correlation between the spectroscopic measurement due to the biochemically and histological methods was obtained. Målet med dette arbeidet var å studere ulike parametre av bindevev med Fourier-transform infrarød (FT-IR) spektroskopi. Disse parametrene er kollagen fiber orientering, kollagen og sulfaterte glykosamineoglykaner (GAGs) mengde, og deres relative ratio under lagring. To ulike bovine muskler ble studert, indrefilet (M. psoas major, PM) og lårtunge (M. semitendinosus, ST). Disse musklene varierer i mørhet, der indrefilet er mørest. Musklene ble lagret ved 4 º i 19 dager, der prøver ble tatt ut hver tredje dag til spektroskopiske, biokjemiske og histologiske analyser. Mekanisk målinger (Warner Bratzer) ble gjort for å bekrefte tekstur egenskaper i de to musklene. Biokjemisk måling med DMB og histologisk farging med Alcian blue ble brukt til å måle innhold og detektere fordelingen av sulfaterte GAGs i de to musklene under lagring. Prøvene ble også farget med kollagen I antistoffer for å se distribusjonen av kollagen I i bindevevet i de to musklene. Prøvene ble målt med FT-IR mikro spektroskopi og ved hjelp av både enkelt spektra og polarisert lysmikroskopi avbilding. Absorbans topper ble analysert i forhold de ulike bindevevsparameterne. De polarisert målingen ble brukt til å undersøke retningen av kollagen fibrene i bindevevet. Absorbans topp ved 1237 cm-1 viste en nedgang i sulfaterte GAGs i begge muskler under lagring, dette i samsvar med biokjemiske og histologiske resultater. Lårtunge hadde et høyere innhold av sulfaterte GAGs enn indrefilet. Lårtunge hadde også en mer markant nedgang som ble sett både i de biokjemiske resultatene og i spektrene. Absorpsjon av collagen ved 1659 cm-1 viste en mulig degradering av kryssbindinger i indrefilet, men ved bruk av en annen kryssbinding ratio (1660:1690) ble ingen forskjell funnet. Absorbansen ved 1654 cm-1 kan indikere en konformasjon endring i kollagen α-helix i indrefilet. To band i vannet regionen viste hydrogenert og ikke-hydrogenert N- H strekk, på henholdsvis ~ 3290 og ~ 3335 cm-1. Disse vann toppene kan brukes til å beregne hydrogenering av bindevevs proteiner og det viser at musklene mister vann gjennom lagring. De polariserte målingene viste at kollagen fibrene i indrefilet hadde en tilfeldig orientering, mens fibre i lårtunge viste en orientering parallelt med x-aksen tidlig i perioden, og en tilfeldig orientering etter 11 dagers lagring.. Farging med antistoffer mot kollagen I støttet disse resultatene, viser en mer tydelig kollagen orientering med ”trådlike” strukturer. Våre resultater fra denne studien viser at FT-IR mikro spektroskopi er lovende i evaluering av bindevevs komponenter i bovine skjelett muskler. Det var god korrelasjon mellom de spektroskopiske og biokjemiske målingene

Raman spectroscopy for quantification of residual calcium and total ash in mechanically deboned chicken meat

According to European food safety authorities, one of the major control parameters for mechanically separated meat is calcium content, which is an indicator of residual bone. Residual bone in mechanically separated meat can also be measured as total ash content. Despite the need to measure both ash and/or calcium content of mechanically separated meat, there is no rapid analytical technique that can be used in an industrial environment. In the current study, we are presenting the first application of Raman spectroscopy as a rapid tool for estimating calcium and ash contents in bone and meat mixtures from mechanical deboning of chicken meat. Raman-based partial least squares regression models were developed for prediction of both ash and calcium content in 79 samples gathered from four different production days. Two different data pre-processing methods, i.e., polynomial background fitting and extended multiplicative scatter correction with polynomial extension, were applied to the raw Raman data and the prediction models were compared. The prediction model based on EMSC treated data afforded the lowest root mean square error of cross-validation (RMSECV=0.333 g/100 g for calcium and RMSECV=0.634 g/100 g for ash) and the highest coefficient of determination (R2=0.775 for calcium and R2=0.894 for ash).acceptedVersio

Collagen from Turkey (Meleagris gallopavo) tendon: A promising sustainable biomaterial for pharmaceutical use

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Estimating dry matter and fat content in Blocks of Swiss cheese during production using on-line near infrared spectroscopy

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Novel NIR Transflection Measurements for Non-contact Core Temperature of processed Meat Products

A novel system for online measurement of core temperature in processed meat products is presented. The system allows near infrared (NIR) light to interact with the product to a depth of up to 2cm using noncontact optics. Two possible meat products were investigated; hot dog and pâté. Both were tested after cooking and chilling. RMSECVs of less than 1.75ºC were obtained for all models and the cooking model for the pâté was tested on 2 different data sets, measured on pâté from a different batch, on a different day and under different conditions to test robustness. The pâté in the test sets was from a different batch and RMSEPS of 1.38ºC and 3.3ºC were obtained for these.pâté. Both were tested after cooking and chilling. RMSECVs of less than 1.75ºC were obtained for all models and the cooking model for the pâté was tested on 2 different data sets, measured on pâté from a different batch, on a different day and under different conditions to test robustness. The pâté in the test sets was from a different batch and RMSEPS of 1.38ºC and 3.3ºC were obtained for these

Novel NIR Transflection Measurements for Non-contact Core Temperature of processed Meat Products

A novel system for online measurement of core temperature in processed meat products is presented. The system allows near infrared (NIR) light to interact with the product to a depth of up to 2cm using noncontact optics. Two possible meat products were investigated; hot dog and pâté. Both were tested after cooking and chilling. RMSECVs of less than 1.75ºC were obtained for all models and the cooking model for the pâté was tested on 2 different data sets, measured on pâté from a different batch, on a different day and under different conditions to test robustness. The pâté in the test sets was from a different batch and RMSEPS of 1.38ºC and 3.3ºC were obtained for these.pâté. Both were tested after cooking and chilling. RMSECVs of less than 1.75ºC were obtained for all models and the cooking model for the pâté was tested on 2 different data sets, measured on pâté from a different batch, on a different day and under different conditions to test robustness. The pâté in the test sets was from a different batch and RMSEPS of 1.38ºC and 3.3ºC were obtained for these

Novel NIR Transflection Measurements for Non-contact Core Temperature of processed Meat Products

A novel system for online measurement of core temperature in processed meat products is presented. The system allows near infrared (NIR) light to interact with the product to a depth of up to 2cm using noncontact optics. Two possible meat products were investigated; hot dog and pâté. Both were tested after cooking and chilling. RMSECVs of less than 1.75ºC were obtained for all models and the cooking model for the pâté was tested on 2 different data sets, measured on pâté from a different batch, on a different day and under different conditions to test robustness. The pâté in the test sets was from a different batch and RMSEPS of 1.38ºC and 3.3ºC were obtained for these.pâté. Both were tested after cooking and chilling. RMSECVs of less than 1.75ºC were obtained for all models and the cooking model for the pâté was tested on 2 different data sets, measured on pâté from a different batch, on a different day and under different conditions to test robustness. The pâté in the test sets was from a different batch and RMSEPS of 1.38ºC and 3.3ºC were obtained for these

Characterization of Collagen Structure in Normal, Wooden Breast and Spaghetti Meat Chicken Fillets by FTIR Microspectroscopy and Histology

Recently, two chicken breast fillet abnormalities, termed Wooden Breast (WB) and Spaghetti Meat (SM), have become a challenge for the chicken meat industry. The two abnormalities share some overlapping morphological features, including myofiber necrosis, intramuscular fat deposition, and collagen fibrosis, but display very different textural properties. WB has a hard, rigid surface, while the SM has a soft and stringy surface. Connective tissue is affected in both WB and SM, and accordingly, this study’s objective was to investigate the major component of connective tissue, collagen. The collagen structure was compared with normal (NO) fillets using histological methods and Fourier transform infrared (FTIR) microspectroscopy and imaging. The histology analysis demonstrated an increase in the amount of connective tissue in the chicken abnormalities, particularly in the perimysium. The WB displayed a mixture of thin and thick collagen fibers, whereas the collagen fibers in SM were thinner, fewer, and shorter. For both, the collagen fibers were oriented in multiple directions. The FTIR data showed that WB contained more β-sheets than the NO and the SM fillets, whereas SM fillets expressed the lowest mature collagen fibers. This insight into the molecular changes can help to explain the underlying causes of the abnormalities.publishedVersio

The use of Fourier‐transform infrared spectroscopy to characterize connective tissue components in skeletal muscle of Atlantic cod (Gadus morhua L.).

In the present study, Fourier‐transform infrared spectroscopy (FTIR) is investigated as a method to measure connective tissue components that are important for the quality of Atlantic cod filets (Gadus morhua L.). The Atlantic cod used in this study originated from a feeding trial, which found that fish fed a high starch diet contained relative more collagen type I, while fish fed a low starch (LS) diet contained relative more glycosaminoglycans (GAGs) in the connective tissue. FTIR spectra of pure commercial collagen type I and GAGs were acquired to identify spectral markers and compare them with FTIR spectra and images from connective tissue. Using principal component analysis, high and LS diets were separated due to collagen type I in the spectral region 1800 to 800 cm−1. The spatial distribution of collagen type I and GAGs were further investigated by FTIR imaging in combination with immunohistochemistry. Pixel‐wise correlation images were calculated between preprocessed connective tissue images and preprocessed pure components spectra of collagen type I and GAGs, respectively. For collagen, the FTIR images reveal a collagen distribution that closely resembles the collagen distribution as imaged by immunohistochemistry. For GAGs, the concentration is very low. Still, the FTIR images detect the most GAGs rich regions.publishedVersio