Amrit Pal Kaur

Effect of liquid whole egg, fat and textured soy protein on the textural and cooking properties of raw and baked patties from goat meat

Abstract Effects of addition of liquid whole egg (LWE), fat and textured soy protein (TSP) on textural and cooking properties of goat meat patties were studied. Textural properties of raw and baked patties were measured using an Instron Universal Testing Machine. Regression models were computed for textural and cooking properties as well as overall acceptability scores of patties as a function of LWE, fat and TSP. TSP showed greatest effect on cohesiveness, puncture force, back extrusion force and hardness of both raw and baked patties. While fat showed the highest effect on gumminess, chewiness and adhesiveness of raw patties, LWE improved the juiciness of the patties, lowered the shrinkage and cooking losses. Addition of TSP significantly decreased overall acceptability of baked patties, particularly at highest addition level (20%). The majority of the models had an R2 over 0.9, indicating they are appropriate and can be used to describe the effect of LWE, fat and TSP on textural and cooking properties of goat meat patties.

Recurrent pregnancy loss: TNF-α and IL-10 polymorphisms.

BACKGROUND: The recurrent pregnancy loss requires careful consideration of genetic, anatomic, endocrine, infectious and immunological factors. Cytokine gene polymorphisms in the promoter regions of tumor necrosis factor (TNF)-α and interleukin (IL)-10 are associated with recurrent pregnancy loss. AIM: The aim of present study was to investigate the association of the IL-10 -592C/A and TNF-α-308 G/A, promoter polymorphisms among women with at least three consecutive miscarriages. MATERIALS AND METHODS: Genotyping was done in 50 women with RPL for IL-10-592C/A and TNF-α-308G/A promoter polymorphism to see the association of these loci with pregnancy loss. The control group included 50 healthy women having two or more children (mean age of the female subjects 35 years) for statistical comparisons. RESULTS: IL- 10-592C/A and TNF-α-308G/A promoter polymorphisms were not associated with the recurrent miscarriages. CONCLUSIONS: There is a need to screen a larger sample and in different ethnic groups using IL-10-592C/A and TNF-α-308G/A markers to understand their association with recurrent miscarriages. This would further help in efficient management of immunologically mediated recurrent miscarriages at the sample/individual level.

Monitoring growth, survival and enzyme system of melon fruit fly Bactrocera cucurbitae (Coquillett) under the influence of affinity purified pea lectin

Pisum sativum agglutinin has been shown to act as a feeding inhibitor for various insect pests belonging to different orders: Lepidoptera, Coleoptera and Hemiptera. In the present study, its insecticidal activity was assessed through monitoring the growth and development of a dipteran pest Bactrocera cucurbitae (Coquillett) (Diptera: Tephritidae). Pea lectin, P. sativum agglutinin (PSA) was purified by single step affinity chromatography on a Sephadex G‐100 and the purification was monitored through hemagglutination activity and SDS‐PAGE. Insect feeding assays were conducted to determine the effect of pea lectin against first and second instar larvae of melon fruit fly B. cucurbitae. Lectin was incorporated in an artificial diet at a varied range of concentrations, 12.5, 25, 50, 100, 200 and 400 μg/mL. The lectin showed highly significant antimetabolic effects in both first and second instars. Time taken for pupation and development as well as percentage pupation and percentage adult emergence were adversely affected. The activity of three hydrolase enzymes (esterases, acid and alkaline phosphatases), five oxidoreductases (superoxide dismutase, catalase, ascorbate peroxidase, peroxidase, O‐demethylase) and one group transfer enzyme (glutathione‐S‐transferases) was also assessed in second instar larvae fed on lectin treated diet at 100 μg/mL concentration. The P. sativum lectin significantly and deleteriously influenced the activity of all these enzymes at all exposure intervals.

Biopotency of partially purified protease inhibitor from peas on the larval growth, development and enzyme system of Bactrocera cucurbitae (Diptera: Tephritidae)

Plant protease inhibitors (PI) constitute a major class of defence proteins being selected as an important strategy towards insect herbivory. With the objective of assessing the effect of PI towards larval growth and development, an artificial diet bioassay using partially purified PI obtained from peas was performed on the melon fruit fly Bactrocera cucurbitae (Coquillett). Larval growth and developmental parameters were assessed at different concentrations (namely 12.5, 25, 50,100, 200 and 400 μg/ml) on the second-instar larvae of B. cucurbitae. Growth and survival responses determined the antiinsect potential of this PI even in its partially purified state. Larval and total development periods were found to be significantly prolonged for the larvae fed on an artificial diet incorporated with pea PI when compared with those fed with a control diet. Furthermore, when compared with the effect of the control diet (no inhibitor), the partially purified pea PI in the diet reduced larval weight gain, mean larval growth rate and food assimilated with respect to the control of the second-instar larvae tested at the same range of concentrations. The relative effectiveness of pea PI on these parameters is in agreement with the results obtained for percentage of pupation and percentage of adult emergence, as these parameters were significantly affected by the increase in the PI concentration in the artificial diet. Feeding the second-instar larvae a diet containing a range of concentrations (50,100,200 and 400 μg/ml) of partially purified pea PI significantly reduced the activities of digestive enzymes (trypsin, chymotrypsin, elastase and leucine aminopeptidase) and significantly affected the activities of other non-digestive enzymes (esterase, acid and alkaline phosphatases, glutathione S-transferase, superoxide dismutase and catalase).