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باراں ماہ ہک بیت وچ

باراں ماہ
(باراں ماہ ہک بیت وچ)

چیتر چائ، وساکھ نوں وس کوئی نہ، جیٹھ جان ہاری وچ ہاڑیاں دے

ہڑاں ہاڑ آئیاں، ساون سانجھ کوئی نہ، بھادوں بھاہ ہوئے ہجر ساڑیاں دے

اسوج آس مکی، کتیں کار بھلے، مگھر ماری گئی وچ پواڑیاں دے

پوہ پیش آئیاں ماگھ مصیبتاں نی، پھگن پھٹ حنیف کوہاڑیاں دے

الالتفات في القرآن الكريم دراسة تحليلية

The paper deals with the different styles  of iltifāt  found in the Holy Qur’ān  and coming out with a general scheme to account for its occurrence in order to enhance the understanding of the subtleties of this feature of Qur’ān ic style. To accomplish this, the research was carried out by way of an analytical study of the instances of iltifāt  in the Holy Qur’ān. As a prelude to the discussion of this subject, the research provides the meaning of iltifāt  among the Arab rhetoricians and the status of iltifāt  as one of the rhetorical tropes. The paper also discussed the significations of iltifāt  which have already been mentioned by previous scholars, and since those scholars touched on the significations only briefly, therefore, the research strived to explore further aspects of their interpretations making an effort to highlight new significations of iltifat and an attempt to introduce a new approach in looking at the iltifāt  phenomenon, in different Sura’hs of          Qur’ān, to demonstrate the application of this new perspective. Finally the research shows that the occurrence of iltifÉt in the Qur’ān  follows certain patterns that are related to the intended significations at the various locations where they appear in the Qur’ān.

Molecular Characterization of Thermostable Cellulase from Thermotoga Naphthophila.

Current study deals with the production, purification and characterization of recombinant thermostable cellulase from Thermotoga naphthophila. PCR using the genomic DNA of T. naphthophila as template resulted in amplification of 1 kb cellulase gene. The amplified cellulase gene was cloned in pTZ57R/T and sub-cloned in pET28a. The expression of recombinant cellulase was analyzed using BL21 CodonPlus (DE3) cells as expression host. The expression studies resulted in the production of recombinant enzyme as soluble protein. The recombinant protein was purified by affinity column chromatography. The characterization studies of purified protein demonstrated the optimal enzyme activity at 90 °C and pH 4.8. The presence of cobalt enhanced the cellulase activity and 2.5 mM cobalt was recorded the optimal concentration for the maximal cellulase activity. SDSPAGE analysis confirmed the molecular weight of recombinant protein as 39 kDa. The protein was found thermostable which retained more than 70% residual activity with an incubation of 1.67 h at 90 °C in the presence of cobalt. Presence of ionic and non-ionic detergents showed an inhibitory effect on the enzyme activity. Kinetic studies of recombinant protein demonstrated the km and Vmax values of 0.22 mg/mL and 2500 µmoles/min respectively using carboxymethyl cellulose as substrate. The deinking potential of recombinant cellulase to remove ink from the paper makes this enzyme a suitable candidate for its use in paper Industry. We are reporting a new member of M42 Family of aminopeptidases. The stability of this recombinant cellulase at wide range of temperature, pH, its high level activity and its paper deinking potential makes it a suitable candidate for its use in paper industry.
Asian Research Index Whatsapp Chanel
Asian Research Index Whatsapp Chanel

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