Heni Rachmawati, Adhitya Jessica, Yeyet Cahyati Sumirtaputra, Debbie Sofie Retnoningrum, Amirah Adlia, Ratih Asmana Ningrum (2016).
Removing a Cystein Group On Interferon Alpha 2b at Position 2 and 99 does Not Diminish Antitumor Activity of the Protein, Even Better.
Scientia Pharmaceutica. 84: 113–130. ISSN 0036-8709 (Print) ISSN 2218-0532 (Online) ISSN-L 0036-8709
Interferon alpha 2b is the only standard therapeutic protein for hepatitis virus infections. Further study demonstrated that this protein also posseses antitumor activity in several cancerous organs. One main pathway of this antitumor activity is mediated through antiproliferation as well as proapoptotic effects. Previously, we have successfully developed recombinant human interferon alpha 2b (rhIFNá2b) by using a synthetic gene. In addition, two mutein forms of rhIFNá2b were generated to improve the characteristics of this protein. Two point mutations showed better pharmacokinetic profiles than one point mutation as well as the native form. In the present study, this mutein form was studied for ist antitumor effect in vitro using HepG2 cells. As a comparison, the native form as well as a commercial rIFNá2b were used. Several parameters were investigated including the MTT assay, cell viability test, cell cycle using flow cytometric analysis, and the genes and protein expressions involved in cell growth. The latest was observed to study the mechanism of rhIFNá2b. There was no significant difference in the MTT assay and cell viability after cells were treated with both forms of rhIFNá2b. However, the mutein rhIFNá2b tended to show better proapoptotic activity reflected by flow cytometric data, protein expression of pSTAT1, and DNA expression of caspase 3.
Keywords: Interferon alpha 2b, Antiproliferation, Apoptosis, p21k1, p27, Caspase 3, pSTAT1, Flow cytometri, Mutein
Urip Perwitasari, Nuryati, Ruth Melliawati, and Yopi (2017). Glucoamylase Production by Aspergillus awamori KT-11 In Solid-State Fermentation Using Cassava Peel as Substrate. Annales Bogorienses, Vol. 21 (1): 21-28. ISSN 0517-8452
Cassava has long been known as one of the main staple food in Indonesia. Whereas the cassava peel contains starch of approximately 72%, it is still underrated as a carbohydrate source for fermentation. The utilization of cassava peel as a substrate in solid state fermentation potentially replaces rice as a carbon source leading to more cost-effective production. This study aims at producing glucoamylase by means of solid state fermentation using Aspergillus awamori KT-11 and cassava peel as substrate. The study demonstrated that medium composition and drying technique affected the production of glucoamylase. The highest glucoamylase activities were identified when cassava peel and mineral media was used in fermentation, compared to only cassava peel; the combination of cassava peel, mineral, and rice bran; rice media or a mixture of rice, mineral and rice bran. Freeze-dried glucoamylase, furthermore, exhibited higher specific activity in contrast to the oven-dried one, with 452 U/mL and 365 U/mL, respectively. In conclusion, cassava peel plus mineral is a better substrate for glucosamine production by A. awamori KT-11 in solid state fermentation. Besides, powdered glucoamylase had been demonstrated to be capable of hydrolyzing starch-based biomass.
Keywords: glucoamylase, cassava peel, A. awamori KT-11, solid state fermentation
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