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- 저자 : Hasan Temiz (검색결과 3 건)
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Hasan Temiz,Kübra Dağyıldız 한국축산식품학회 2017 한국축산식품학회지 Vol.37 No.4
The objective of this research was to investigate the effects microbial transglutaminase (m- TGs) on the physicochemical, microbial and sensory properties of kefir produced by using mix cow and soymilk. Kefir batches were prepared using 0, 0.5, 1 and 1.5 Units m-TGs for per g of milk protein. Adding m-TGs to milk caused an increase in the pH and viscosity and caused a decrease in titratable acidity and syneresis in the kefir samples. Total bacteria, lactobacilli and streptococci counts decreased, while yeast counts increased in all the samples during storage. Alcohols and acids compounds have increased in all the samples except in the control samples, while carbonyl compounds have decreased in all the samples during storage (1-30 d). The differences in the percentage of alcohols, carbonyl compounds and acids in total volatiles on the 1st and the 30th d of storage were observed at 8.47-23.52%, 6.94-25.46% and 59.64-63.69%, respectively. The consumer evaluation of the kefir samples showed that greater levels of acceptability were found for samples which had been added 1.5 U m-TGs for per g of milk protein.
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The Partial Purification and Properties of Pepsin Obtained from Turkey Proventriculus
Temiz, Hasan,Aykut, Umut,Okumus, Emin,Turhan, Sadettin Korean Society for Biotechnology and Bioengineerin 2007 Biotechnology and Bioprocess Engineering Vol.12 No.4
In this study, pepsin from turkey proventriculus was purified, and its biochemical properties examined. Initially, the turkey proventriculus (stomach) was mixed with 10% NaCl (1:2, w/v) and extracted by centrifugation to produce a crude extract. The partial purification of the extract was carried out using Sephadex G-50 resin in gel filtration column chromatography. The fractions obtained by gel filtration were analyzed for milk clotting activity (MCA), protein content, proteolytic activity (PA), purification factor (PF), and SOS-PAGE electrophoresis was also performed. The enzyme was purified 207-fold with a recovery of 36%. The first 4 fractions did not have any activities; fractions 7, 8, and 9 exhibited the highest levels of milk clotting and proteolytic activity. The electrophoretic patterns revealed that further purification steps should be applied for better results.
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The Partial Purification and Properties ofPepsin Obtained from Turkey Proventriculus
Sadettin Turhan,Hasan Temiz,Umut Aykut,Emin Okumus 한국생물공학회 2007 Biotechnology and Bioprocess Engineering Vol.12 No.4
In this study, pepsin from turkey proventriculus was purified, and its biochemical properties examined. Initially, the turkey proventriculus (stomach) was mixed with 10% NaCl (1:2, w/v) and extracted by centrifugation to produce a crude extract. The partial purification of the extract was carried out using Sephadex G-50 resin in gel filtration column chromatography. The fractions obtained by gel filtration were analyzed for milk clotting activity (MCA), protein content, proteolytic activity (PA), purification factor (PF), and SDS-PAGE electrophoresis was also performed. The enzyme was purified 207-fold with a recovery of 36%. The first 4 fractions did not have any activities; fractions 7, 8, and 9 exhibited the highest levels of milk clotting and proteolytic activity. The electrophoretic patterns revealed that further purification steps should be applied for better results.
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