Kenevir tohum proteinlerinin ultrases, yüksek basınç ve manotermosonikasyon uygulamaları ile modifikasyonu
Modification of hemp seed proteins using ultrasound, high pressure and manotermosonication treatments
- Tez No: 798087
- Danışmanlar: DOÇ. DR. OKTAY YEMİŞ
- Tez Türü: Doktora
- Konular: Gıda Mühendisliği, Food Engineering
- Anahtar Kelimeler: Belirtilmemiş.
- Yıl: 2023
- Dil: Türkçe
- Üniversite: Sakarya Üniversitesi
- Enstitü: Fen Bilimleri Enstitüsü
- Ana Bilim Dalı: Gıda Mühendisliği Ana Bilim Dalı
- Bilim Dalı: Gastronomi Bilim Dalı
- Sayfa Sayısı: 146
Özet
Dünya nüfusundaki hızlı artış trendi gelecekte gıda talebini karşılamada zorluklar yaşanacağına işaret etmektedir. Ayrıca, küresel salgınlar, savaşlar ve iklim değişiklikleri gıda zincirindeki olası sıkıntıları tetiklemektedir. Bu noktada sağlıklı beslenme düzeninde kilit rol oynayan proteinlerin tedariğinde yakın gelecekte sıkıntılar meydana geleceği öngörülmektedir. Özellikle hayvansal protein kaynaklarıyla ilişkili ekonomik, etnik ve dini nedenlere ek olarak bu kaynakların yarattığı çevre ve sağlık endişeleri araştırmacıları alternatif protein kaynakları üzerinde çalışmaya yönlendirmiştir. Bu bağlamda, bitkisel protein kaynakları bol, çeşitli, ucuz ve erişilebilir olmasıyla küresel markette hızlı bir şekilde yer edinmiştir. Artan tüketici bilinciyle birlikte sağlıklı, dengeli ve vejetaryen beslenmeye eğilim bitkisel protein talebine ivme kazandırmıştır. Özellikle gıda işleme atıklarının alternatif protein kaynağı olarak değerlendirilmesi, çevresel geri dönüşümü destekleyerek sürdürülebilir, katma değerli ve yenilikçi çözümler üretmesiyle önem taşımaktadır. Kenevir; lifi, tohumu ve yağı için uzun yıllardan beri yetiştirilen çok fonksiyonlu endüstriyel bir bitkidir. Son yıllarda yapılan yasal düzenlemelerle uyuşturucu (Marijuana) ve endüstriyel kenevir çeşitlerinin (Cannabis sativa, d–9–tetrahidrokannabinol (THC)
Özet (Çeviri)
The global population is anticipated to reach 10.4 billion by 2100, which will result in considerable challenges to meet the protein demand in future. Furthermore, the COVID-19 pandemic has markedly expedited the transition to alternative protein sources, owing to the disruption in the worldwide food supply chain. Recent studies have reported the favorable impact of plant-based diets on mitigating the severity of COVID-19. Plant proteins have been attracting attention due to various reasons, such as economic, ethnic, and religious factors, as well as consumers' growing awareness of sustainable and healthy diet. All these factors have led to increase the popularity of plant-based products, which have become more readily accessible, diverse, and affordable in the market. The global plant protein market's worth was $12.2 billion in 2022, with a projected Compound Annual Growth Rate (CAGR) of 7.3% over the next five years. The escalating demand has triggered the pursuit of utilizing industrial plant waste, which was previously considered an environmental problem or used as animal feed, as an alternative, low-cost, and clean-labeled protein source. Hemp seed, an industrial by-product, has garnered substantial attention in recent years due to its rich protein and oil content. Hemp seed protein (HSP) is recognized for its high digestibility, low allergenicity, and bioactive properties. Cannabis sativa L. (C. sativa L.), a hemp variety containing a low amount of d–9–tetrahydrocannabinol (THC) (0.2%), is typically classified into two different types. As the demand for hemp fiber from industries such as paper, biodegradable plastics, textiles, and fuel continues to increase, so does the quantity of hemp seeds that are discarded as waste. Hemp seed is a superb by-product, with high-quality protein (20–25%) and oil (30–35%). The meal obtained from the seeds after hemp oil extraction contains roughly 55–60% protein. Comparisons of hemp seed proteins with egg white and soy protein in terms of nutritional value and digestibility have indicated that hemp protein can be an alternative food additive. Additionally, hemp seeds exhibit favorable health effects, including the ability to reduce blood pressure and cholesterol levels. This PhD thesis focused on evaluating the efficacy of non-thermal and chemical modification techniques, both separately and in combination, for enhancing the functional properties of hemp seed proteins. Ultrasound homogenization (USH), high pressure homogenization (HPH), manothermosonication (MTS) from non-thermal techniques, and pH shifting from chemical techniques were considered to investigate their effects on the functional, physicochemical, morphological, and bioactive properties of hemp seed proteins. Ultrasound homogenization (USH) is a non-thermal technique based on a combination of effects such as cavitation, heating, dynamic agitation, shear stresses, and turbulence. Cavitation bubbles, microjets, micro-turbulence, high-speed interparticle collisions, and microporous particle disruption cause modifications. The bursting of these bubbles generates high temperature and pressure values (approximately 50 MPa and 5500 K) around the bubble, leading to several reactions in the solution. In the first part of the thesis, the optimal processing conditions for the USH treatment were determined as 6.9% protein concentration (at a frequency of 20 kHz), 37 W/cm2 acoustic intensity, and 7.8 minutes processing time based on maximum solubility and minimum particle size responses of HSP. The solubility and particle size responses were used to obtain models with high R2 and lack-of-fit values. After USH treatment, the solubility of HSP (78%), free SH group content (59%), and zeta potential increased (25%), while the particle size decreased (46%). Although there was no significant change in the electrophoretic profile of HSP-USH under optimum conditions, the amino acid profile of HSP-USH differed from that of HSP. Moreover, the emulsification, oil absorption, and foaming properties of HSP-USH were found to increase compared to HSP, while the lowest gel concentration decreased. The shift in the amide 1 (1700–1600 cm-1) region from 1636 cm-1 to 1629 cm-1 after USH application indicates a partial alteration in the secondary structure of HSP. The amide 2 region (1580–1480 cm-1) is characterized by dominant N–H (40-60%), C–N (18-40%), and C–C (10%) vibrations. The shift in the peak number from 1529 cm-1 to 1524 cm-1 in the Amid 2 region (1580–1480 cm-1) of HSP indicates alterations in α-helix and β-sheet structures. The shifts towards higher values suggest the transformation of the protein into random coil and β-sheet structures following USH application. After USH treatment, an increase in the denaturation temperature and proportion of β-structure for the secondary structure distribution was observed. Furthermore, the USH treatment led to a 38% increase in the antioxidant properties of HSP. The aim of the second part is to examine the impact of high-pressure homogenization (HPH) and manothermosonication (MTS) processes, as well as their combined employment with pH-shift treatments, on the physicochemical, morphological, and functional attributes of hemp seed proteins. The MTS represents an innovative technology in which ultrasound homogenization (USH) technology is integrated with pressure and temperature application in a continuous system. While the alone-USH technology cannot yield the desired protein alterations, this limitation can be surmounted using integrated systems. Moreover, the efficacy of USH application is restricted by the requirement of an extended processing time of up to 15–30 minutes, thereby hindering its industrial applicability. In contrast, the MTS system has reduced the processing time from 15.9 minutes to 1.4 minutes, providing similar results with a more moderate temperature application. This makes it a more feasible and efficient alternative to thermal modification approaches. Chemical modification of proteins can be achieved through various techniques (phosphorylation, Acylation, pH-shifting, etc.), which pH shifting stands out as a straightforward and safe approach among these techniques. Extensive studies have shown that polypeptide structures of proteins can be altered by exposing them to highly acidic or alkaline pH treatments (pH 1.5–3.5 or pH 10–12). The rationale behind this is that the polypeptide chains of proteins unfold at extreme pH levels and subsequently refold and rearrange when the pH is adjusted to 7.0. The pH shifting process induces partial denaturation, resulting in tertiary structure losses, side chain interactions, and the release of sulfhydryl and hydrophobic nuclei, leading to the formation of“molten globules.”To enhance the modification of proteins, researchers often combine the pH shifting technique with thermal or non-thermal technologies. One such non-thermal technique is high-pressure homogenization (HPH), which has gained popularity in the food industry and among researchers for its ability to modify the molecular structure, functionality, and physicochemical properties of proteins. HPH operates on the principle of subjecting a suspension to high pressure, causing it to flow continuously through a narrow valve, resulting in high turbulence, shear stress, cavitation, and a rise in temperature. The optimal parameters for the MTS process were determined to be 50°C, 200 kPa, and 90 s, based on the highest solubility and the lowest particle size. The solubility of pH12MTS isolate increased by 52% compared to untreated HSP. Furthermore, the emulsion activity and stability of pH12MTS isolate exhibited the highest values with 2.11- and 2.15-fold increases, respectively, compared to HSP. The particle size decreased from 365.87 nm to 112.67 nm following pH12MTS treatment. The zeta potential, free SH group content, and fluorescence intensity of the modified isolates increased due to the combined effects of cavitation forces and pH shifting treatments, providing evidence of tertiary structural changes. After the applied modification processes, a change in the secondary structure of HSP was observed, which was evidenced by the decrease of α-helix forms and the increase of random coil forms as a result of FTIR and CD data. The secondary structural distribution of the HSP sample was found to be 4.5% α-helix, 37.9% β-sheet, 14.7% β-turn, and 42.9% random coil. As a general trend, the ratio of α-helix and β-sheet decreased, while the ratio of β-turn and random coil increased in the secondary structure composition of all treated samples. The change in secondary structure indicated that the possibility of a reversal from α-helix and β-sheet to β-turn and random coil. After the modification applications, the FImax value of HSP increased from 13768 Au to 43268 Au for pH12MTS. The pH12MTS isolate demonstrated the highest fluorescence intensity compared to the other isolates, followed by the fluorescence intensity values of HPH, MTS, pH12HPH, and pH12 isolates, respectively. While the λmax value was approximately 334 nm for untreated HSP, all modified isolates exhibited shifts towards longer wavelengths (336 nm). These shifts towards longer wavelengths are known as bathochromic shifts or redshifts. The bathochromic shift is caused by the surface orientation of the tryptophan embedded in the interior of the protein and the increase in polarity in the liquid medium. In addition, all applications changed the thermal behavior of the isolates and the proportional distribution of the crystal structure, causing the modified HSP to exhibit more irregular forms. After the modification processes, the digestibility of HSP increased from 84.23% to 95.46% after pH12MTS treatment. In summary, this PhD thesis has established that various non-thermal and chemical modification techniques can significantly enhance the technological properties of hemp seed protein. The study has highlighted that optimal process parameters are critical for obtaining the desired functional properties. Compared to the conventional USH process, the MTS method provided a more effective modification with a shorter processing time. The modified hemp seed proteins exhibit potential as multi-functional food ingredients, offering desirable techno-functional properties for food products. Additionally, the USH, HPH, and MTS technologies employed in this research can be applied to obtain functionalized, value-added protein ingredients, encapsulation, and biopolymer packaging materials.
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