Response surface optimization of protein extraction from cold‐pressed terebinth (Pistacia terebinthus L.) oil byproducts: Physicochemical and functional characteristics

• Published in: Journal of food science Vol. 89; no. 11; pp. 7380 - 7396
• Main Authors: Ozgolet, Muhammed, Cakmak, Zeynep Hazal Tekin, Bozkurt, Fatih, Sagdic, Osman, Karasu, Salih
• Format: Journal Article
• Language: English
• Published: United States Wiley Subscription Services, Inc 01-11-2024
• Subjects: Absorption; By products; Byproducts; Digestibility; emulsifying properties; Foaming; foaming capacity and stability; Isoelectric points; Oils & fats; Optimization; optimization of protein extraction; Parameters; pH effects; Proteins; Purity; response surface; Response surface methodology; terebinth oil byproduct; Thermal stability; Zeta potential; foaming capacity and stability; terebinth oil byproduct; optimization of protein extraction; emulsifying properties; response surface
• ISSN: 0022-1147; 1750-3841; 1750-3841
• DOI: 10.1111/1750-3841.17441

The current study focused on optimizing the extraction parameters of terebinth seed proteins from cold‐pressed terebinth oil byproducts to maximize protein purity and protein yield. The isolated proteins were characterized to evaluate their properties; thus revealing the valorization potential of these byproducts. Response surface methodology was used to detect the effect of three extraction parameters (pH, temperature, and time). The protein isolates were studied for their physicochemical and functional characteristics. The results indicated that an extraction pH of 8, a temperature of 50°C, and an extraction period of 60 min are optimum conditions for obtaining protein isolates with the highest purity. On the other hand, it was demonstrated that an extraction pH of 12, a temperature of 46.4°C, and an extraction duration of 102.4 min were optimum conditions for the maximum protein yield. The proteins produced under these two sets of conditions, referred to as TRP (terebinth protein with maximum purity) and TRY (terebinth protein with maximum yield), respectively, exhibited comparable oil absorption capacity (OAC), foaming, emulsifying capabilities, and stability. Both proteins showed the highest solubility at pH 11, and their zeta potentials approached zero at pH 4, indicating proximity to their isoelectric points. However, FRAP and DPPH assays showed that TRP and TRY offered low antioxidative capacity. The high β‐sheet content in TRP and TRY suggests enhanced thermal stability but reduced digestibility of these proteins. Therefore, in addition to protein enrichment, TRP and TRY protein isolates can be utilized in muffins and other food applications thanks to their favorable oil absorption, foaming and emulsifying capacities, and thermal stabilities.