ArticleMolecules (Basel, Switzerland)2011
Optimization of the conditions for extraction of serine protease from kesinai plant (Streblus asper) leaves using response surface methodology.
Article in Molecules (Basel, Switzerland), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Exploring the Antibiotic Potential of a Serine Protease fromInfectious disease reports · 2025Article
- Production of Plant Proteases and New Biotechnological Applications: An Updated Review.ChemistryOpen · 2022Review
- Partial characterization of an enzymatic extract from Bentong ginger (Zingiber officinale var. Bentong).Molecules (Basel, Switzerland) · 2014Article
- Ultrasonic extraction of antioxidants from Chinese sumac (Rhus typhina L.) fruit using response surface methodology and their characterization.Molecules (Basel, Switzerland) · 2014Article
- Response surface modeling and optimization of ultrasound-assisted extraction of three flavonoids from tartary buckwheat (Fagopyrum tataricum).Pharmacognosy magazine · 2013Article
- Optimization of ultrasonic assisted extraction of antioxidants from black soybean (Glycine max var) sprouts using response surface methodology.Molecules (Basel, Switzerland) · 2013Article
- 'Heat-treatment aqueous two phase system' for purification of serine protease from Kesinai (Streblus asper) leaves.Molecules (Basel, Switzerland) · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Response surface methodology (RSM) using a central composite design (CCD) was employed to optimize the conditions for extraction of serine protease from kesinai (Streblus asper) leaves. The effect of independent variables, namely temperature (42.5,47.5, X₁), mixing time (2-6 min, X₂), buffer content (0-80 mL, X₃) and buffer pH (4.5-10.5, X₄) on specific activity, storage stability, temperature and oxidizing agent stability of serine protease from kesinai leaves was investigated. The study demonstrated that use of the optimum temperature, mixing time, buffer content and buffer pH conditions protected serine protease during extraction, as demonstrated by low activity loss. It was found that the interaction effect of mixing time and buffer content improved the serine protease stability, and the buffer pH had the most significant effect on the specific activity of the enzyme. The most desirable conditions of 2.5 °C temperature, 4 min mixing time, 40 mL buffer at pH 7.5 was established for serine protease extraction from kesinai leaves.
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