Effect of heat shock protein 27 on the in vitro degradation of myofibrils by caspase‐3 and μ‐calpain

This study was designed to investigate the effect of heat shock protein 27 (HSP27) on the in vitro degradation of myofibrils induced by caspase‐3 or μ‐calpain. Myofibrillar proteins were prepared from at‐death beef muscles and incubated with caspase‐3 or μ‐calpain with and without HSP27, or with HSP27 alone, at 30 °C for 2 h, and protein degradation was assessed. Results showed that caspase‐3 promoted the degradation of titin, nebulin and troponin‐T, and μ‐calpain promoted the degradation of nebulin, desmin and troponin‐T, observed during normal PM ageing. Moreover, the addition of HSP27 restricted the degradation of troponin‐T in μ‐calpain‐ and caspase‐3‐treated myofilaments, and restricted the degradation of desmin in μ‐calpain‐treated myofilaments. Therefore, HSP27 may indirectly or directly interact with caspase‐3 and μ‐calpain, reducing their activity and mediating PM proteolysis of muscle proteins to affect meat tenderisation.     

Study on microwave‐accelerated casein protein grafted with glucose and β‐cyclodextrin to improve the gel properties

The effect of glycosylation treatment coupled with microwave heating (MH) on gel properties and structure change of casein were investigated. Conjugation was confirmed by electrophoresis. Protein disulphide bonds were broken by microwave irradiation to create an increase first and a decrease later in free sulfhydryl contents with time, thereby inducing subunit disaggregation. Also, the exposure of hydrophobic core residues was increased in MH‐treated casein, which brings about protein disaggregation and unfolding. It showed that graft reactions by MH had much faster than those by water bath heating (WH). The content of disulphide bonds is 7.2% and 6.0% in the casein–glucose and casein–β‐cyclodextrin, respectively, treated by MH which was reduced significantly than that of treated by WH. Moreover, MH can increase the hardness of the gel. Consequently, MH could improve the efficiency of the reaction and gel properties.     

Effect of succinylation on the functional and physicochemical properties of α‐globulin,the major protein fraction from Sesamum indicum L.

α‐Globulin the major protein fraction fromSesamum indicum was succinylated to different levels and the effect of the chemical modification was evaluated both on the functional and physicochemical properties. The results suggest that the pH of minimum solubility shifted to the more acidic side (pH ˜ 4.5–5.5) for the succinylated α‐globulin whereas for control α‐globulin the pH of minimum solubility was 6.5. Succinylation also increased emulsion activity and emulsion stability of the protein. The emulsion stability increased from a control value of 53 ± 3 s to a value of 122 ± 5 s. Bulk density, water absorption capacity, oil absorption capacity, foam capacity and foam stability were evaluated in phosphate buffer (pH 7.0) containing 0.5 M sodium chloride and all these properties showed increased values as a result of succinylation. Ultracentrifugation studies showed that the % composition of 7S component increases with concomitant decrease in that of 11S fraction with the increase in percentage of succinylation. Further increase in succinylation resulted in only 2S component which is a dissociated form of 11S and/or 7S protein fractions. The fluorescence emission studies showed a decrease in the fluorescence emission intensity of α‐globulin as a result of succinylation. The thermal stability of the protein molecule decreased due to progressive succinylation as indicated by decrease in the apparent thermal denaturation temperature from a control value of 84 to 62°C at a succinylation level of 40%. These results suggest that succinylation improves the functional characteristics of α‐globulin. Such changes in the functional properties have been attributed partly to the dissociation of the protein molecule at higher levels of succinylation and the increase in the net negative charge on the protein.     

A survey and analysis of the role of molecular chaperone proteins and imidazole‐containing dipeptide‐based compounds as molecular escorts into the skin during stress,injury, water structuring and other types of cutaneous pathophysiology

Molecular chaperone, heat shock proteins (HSPs), stabilizes intracellular processes of cells under stress. Little is known about the role of molecular chaperone proteins in the skin pathology, rejuvenation and wound healing, or whether their expression is altered by environmental and physiological stress to the skin or systemic disease. The focus of this study was to examine the role of molecular chaperone proteins in the skin’s local response to wounding, skin ageing and a range of skin diseases. Free radicals, one form of insult, induce or contribute to adverse effects on the skin, including erythema, oedema, wrinkling, photoaging, inflammation, autoimmune reactions, hypersensitivity, keratinization abnormalities, preneoplastic lesions and skin cancer. A unified view of the molecular and cellular pathogenesis of the skin age‐related pathology conditions has led to the search for molecular and chemical chaperones that can slow, arrest or revert disease progression. Specific alpha‐crystallin domains and pharmacological imidazole‐containing dipeptide chaperone molecules are now emerging that link our biophysical insights with developed skin therapeutic techniques. In this article, we discuss the molecular nature of the stress signals, the mechanisms that underlie activation of the heat shock response, the role of molecular chaperone proteins as skin protective molecules, and strategies for pharmacologically active chaperone molecules and their imidazole‐containing dipeptide inducers as regulators of the skin stress response. We discuss how impairment in protein hydration may cause ultrastructural, mechanical and biochemical changes in structural proteins in the aged skin. We have pioneered the molecular chaperone protein activated therapeutic or cosmetic platform to enable simultaneous analysis of water‐binding and structuring characteristics for biology of skin ageing and skin disease‐related pathways. This cutting‐edge technology has improved the way that proteins hydrate in photoaged skin. The mechanisms of skin diseases, ageing, cellular, and signalling pathways mediated by targeting with molecular chaperone protein(s) in patented formulations with imidazole containing dipeptide (N‐acetylcarnosine, carcinine, carnosine) are also discussed within this review.     

Effect of treatment with α‐galactosidase,tannase or a cell‐wall‐degrading enzyme complex on the nutritive utilisation of protein and carbohydrates from pea (Pisum sativum L.) flour

The effect of treatment with α‐galactosidase, tannase or a cell‐wall‐degrading enzyme complex under optimal conditions of pH, temperature and length of incubation time on the chemical composition and nutritive utilisation of protein and carbohydrates from pea (Pisum sativum L.) flour was studied. Soaking of pea flours in combination with enzyme treatment led to reductions of 77–90% in the levels of α‐galactosides, and of 60–80% in the levels of trypsin inhibitor activity, increasing the content of total available sugars, which was highest in the pea flour treated with the cell‐wall‐degrading enzyme complex. All the treatments assayed caused a significant improvement in daily food intake, whereas the nutritive utilisation of protein was not increased in any of the pea products tested when compared to the raw pea flour. However, all the soaking and enzymatic treatments led to a significant improvement in daily weight gain associated with a higher dietary intake of food and total available sugars. Copyright © 2007 Society of Chemical Industry     

The chemistry and medicinal uses of the underutilized Indian fruit tree Garcinia indica Choisy (kokum): A review

Garcinia indica Choisy Syn Brindonia indica, commonly known as kokum and belonging to Guttiferae family, is a plant native to certain regions of India. The trees yield fruits annually in the summer season during the months of March to May. The fruits are green when raw and red to dark purple when fully ripe. They are used to prepare juice, pickles and as acidulant in curries. In the traditional Indian system of medicine the Ayurveda and in various folk systems of medicine, the fruit rinds and leaves are used to treat various inflammatory ailments, rheumatic pain and bowel complaints. The kokum butter prepared from the seed is of both commercial and medicinal use. Chemical studies have shown that the rind contains protein, tannin, pectin, sugars, fat, organic acids like (−)-hydroxycitric acid, hydroxycitric acid lactone and citric acid; the anthocyanins, cyanidin-3-glucoside and cyanidin-3-sambubioside; and the polyisoprenylated phenolics garcinol and isogarcinol. Preclinical studies have shown that kokum or and some of its phytochemicals possess antibacterial, antifungal, anti-ulcerogenic, cardioprotective, anticancer, chemopreventive, free radical scavenging, antioxidant and anti-obesity effects. The present paper reviews the nutritional value, the phytochemical compounds, traditional uses and validated pharmacological properties of kokum.