A modified ninhydrin colorimetric analysis for amino acids

Rosen, Harvey M.

doi:10.1016/0003-9861(57)90241-2

Cited by 2,141 publications

(686 citation statements)

References 5 publications

Supporting

Mentioning

675

Contrasting

Unclassified

Order By: Relevance

“…The distillation method of Tarladgis et al (1960) was followed to determine2-thio barbituri acid reacting substances (TBARS) number and Tyrosine value was estimated by the procedure of Strange et al (1977). Free amino acids were determined by the method of Rosen (1957) in protein nitrogen fraction by ninhydrin reagent. Nit rite content, moisture, protein and fat were determined as per the procedure outlined by AOAC (1995).…”

Section: Texture Profile Analysismentioning

confidence: 99%

Quality and shelf life of buffalo meat blocks processed in retort pouches

et al. 2013

View full text Add to dashboard Cite

The shelf life of buffalo meat blocks processed in 3-ply retort pouches at F o 012.13 in a stock sterilizer were evaluated at 15 days interval for physico-chemical, microbiological and sensory attributes for a period of 3 months. The pH of the product was 6.28 at 0 day and a gradual decline was noticed during storage. Texture of the product as indicated by shear force values had decreased slowly. The residual nitrite content had significantly declined from 82.67 ppm at 0 day to 45.00 ppm on 90th day of storage. The TBARS values were 0.24 and 0.67 mg malonaldehyde/ kg, respectively at 0 day and 90 days of storage. Tyrosine value had significantly increased from 0.37 mg/100 g at 0 day to 0.58 mg/100 g during storage. Free aminoacid content increased gradually from an initial level of 124.32 to 217.51 at 90 th day of storage. The SDS-PAGE hydrolysis pattern showed barely discernible 205 KDa protein and presence of subfragments in the molecular range of 63 KDa to 29 KDa protein. The sensory studies indicated that the products were well acceptable up to a period of 90 days. As the storage period increased pH, reidual nitrite, sensory attributes declined significantly and TBARS value, tyrosine value and free aminoacid content significantly increased. Mesophillic aerobes and anerobes were found to be absent. The shelf life study indicated that the products were well acceptable up to a period of 90 days based on the assessment of physico-chemical, microbiological and sensory attributes.

show abstract

Section: Texture Profile Analysismentioning

confidence: 99%

Quality and shelf life of buffalo meat blocks processed in retort pouches

et al. 2013

View full text Add to dashboard Cite

show abstract

“…735). Amino acids were estimated by the ninhydrin method following the procedure of Rosen (1957). Glycogen in liver homogenates was assayed as glucose following treatment with amyloglucosidase (Roehrig and Allred, 1974).…”

Section: Assay Proceduresmentioning

confidence: 99%

Divergence of endocrine and metabolic responses to stress in two rainbow trout lines selected for differing cortisol responsiveness to stress

Trenzado

Carrick

Pottinger

2003

General and Comparative Endocrinology

View full text Add to dashboard Cite

Abstract. Rainbow trout (Oncorhynchus mykiss) of two lines selected for low (LR) and high (HR) cortisol stress-responsiveness were subjected to confinement for a period of 336 hours.Endocrine (plasma cortisol, hepatic cortisol binding) and metabolic (plasma glucose, lactate, amino acids; hepatic glycogen and alanine aminotransferase levels) indices of stress were measured at intervals in confined and unconfined fish of both lines. During confinement plasma cortisol concentration reached maximum values earlier in HR fish (2 hours) than in LR fish (6 hours) returning to control values within 336 hours in both lines. Paradoxically, although both HR and LR lines displayed a characteristic metabolic stress response, these changes were more pronounced in LR fish. Plasma glucose and lactate levels increased during confinement in both lines but to a significantly greater extent in LR fish. Confinement significantly elevated plasma amino acids to a greater extent in LR fish than in HR fish. Liver glycogen concentration was depleted most rapidly in LR fish but was significantly higher in confined fish of both lines than controls at the end of the experiment. No significant changes were observed in hepatic alanine aminotransferase activity during confinement. Confined fish of both lines displayed a decrease in hepatic cortisol receptor abundance within 24 h and this was more sustained in HR fish. The more pronounced disturbance of a broad range of indicators of stress in confined LR fish, compared to HR fish, throws doubt on the magnitude of the cortisol response being the primary driver of these differences.

show abstract

“…The standard reaction mixture, containing 25 mg collagen (type I and V, from bovine Achilles tendon) in 5 mL of 0.05 M Tris-HCl buffer (pH 7.0), was incubated with 1 mL enzyme samples at 37ºC. The amount of free amino groups released was measured by the ninhydrin method of Rosen (1975). One activity unit (U) was defined as the number of µmol of Lleucine released as a result of the action of 1 mL culture filtrate containing collagenolytic enzyme, after 18 h at 37ºC.…”

Section: Substrate Specificitymentioning

confidence: 99%

Production and Characterization of Collagenase by Penicillium sp. UCP 1286 Isolated From Caatinga Soil

2016

J App Biol Biotech

View full text Add to dashboard Cite

A new Penicillium sp. strain isolated from the soil of Caatinga, a Brazilian Biome (UCP 1286) was selected for collagenase production. Fermentation system allowing obtention of collagenolytic activity about 2.7 times higher than existing data, with the highest values of collagenolytic and specific activity (379.80 U/mL, 1460.77 U/mg, respectively), after 126 hours. Applying a factorial design, enzyme production was increased by about 65% compared to the preliminary results. The factorial design demonstrated the existence of two factors with statistical significance on the production of the enzyme: pH and temperature, both with negative effects. Enzyme was found to be more active at pH 9.0 and 37 °C, and also to be very stable in comparison with the collagenase produced by other microorganisms. The enzyme seems to belong to collagenolytic serine proteases family. Concerning the substrate specificity, it was observed that the highest enzyme activity corresponds to azocoll, there was no relevant activity on azocasein and the enzyme showed to be more specific to type V collagen and gelatin than the commercial colagenase produced by Clostridium histolyticum. Major band observed at electrophoresis was approximately 37 kDa. Zymogram analysis confirmed the collagenolytic activity. All data indicates this enzyme as promising biotechnology product.

show abstract

A modified ninhydrin colorimetric analysis for amino acids

Cited by 2,141 publications

References 5 publications

Quality and shelf life of buffalo meat blocks processed in retort pouches

Quality and shelf life of buffalo meat blocks processed in retort pouches

Divergence of endocrine and metabolic responses to stress in two rainbow trout lines selected for differing cortisol responsiveness to stress

Production and Characterization of Collagenase by Penicillium sp. UCP 1286 Isolated From Caatinga Soil

Contact Info

Product

Resources

About