Enzymatic Hydrolysis of Proteins

Zarei, Mohammad; Muhialdin, Belal J.; Hassanzadeh, Kambiz; Yea, Chay Shyan; Ahmadi, Raman

doi:10.1201/9781003106524-13

Cited by 4 publications

(8 citation statements)

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“…It is an aspartic endopeptidase and has broad cleavage specificity. Pepsin preferentially cleaves peptide bonds between hydrophobic amino acids and produces smaller peptides [ 11 ]. In the pH range of 2 to 5, active pepsin is stable.…”

Section: Introductionmentioning

confidence: 99%

Freeze-Dried Tuna Pepsin Powder Stabilized by Some Cryoprotectants: In Vitro Simulated Gastric Digestion toward Different Proteins and Its Storage Stability

Patil

Nikoo

Zhang

et al. 2022

Foods

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The impact of maltodextrin (10%) in combination with trehalose or glycerol at different levels (2.5% and 5%) and their mixture on the stability of freeze-dried pepsin from skipjack tuna stomach was studied. Addition of 5% trehalose and 10% maltodextrin yielded the powder (TPP-T5) with highest relative pepsin activity (p < 0.05). TPP-T5 had different shapes and sizes, with mean particle size of 65.42 ± 57.60 μm, poly-dispersity index of 0.474, and zeta potential of −19.95. It had bulk density of 0.53 kg m−3 and possessed fair flowability. The wetting time for TPP-T5 was 16.36 ± 0.73 min, and solubility was 93.58%. TPP-T5 stored at room temperature under different relative humidities could maintain proteolytic activity up to 4 weeks. Commercial porcine pepsin (CP) and crude tuna pepsinogen had molecular weights of 35.2 and 43.3 kDa, respectively, when analyzed using gel filtration (Sephadex G-50) and SDS-PAGE. Tuna pepsin had comparable hydrolysis toward threadfin bream muscle protein, whey protein isolate, and kidney bean protein isolate to commercial pepsin, especially at a higher level (15 units/g protein). Digested proteins contained peptides with varying molecular weights as determined by MALDI-TOF. Therefore, pepsin from skipjack tuna stomach could replace commercial porcine pepsin and was beneficial supplement for patients with maldigestion, particularly the elderly.

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Section: Introductionmentioning

confidence: 99%

Freeze-Dried Tuna Pepsin Powder Stabilized by Some Cryoprotectants: In Vitro Simulated Gastric Digestion toward Different Proteins and Its Storage Stability

Patil

Nikoo

Zhang

et al. 2022

Foods

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“…Since the trypsin enzyme cuts after the amino acids lysine and arginine, 6 a beam dependent on the amount of tyrosine cannot be observed. Activity of trypsin was determined by spectrophotometric measurements using BAPNA ( N ‐benzoyl‐1‐arginine‐ p ‐nitroanilide) as a substrate 21,22 …”

Section: Methodsmentioning

confidence: 99%

“…Since the cut‐off point of pepsin enzyme is after tyrosine, phenylalanine and tryptophan amino acids, 6 specific activity of pepsin was measured using spectroscopic method depending on the amount of tyrosine 23…”

Section: Methodsmentioning

confidence: 99%

“…In addition, proteolytic enzymes that split amino acids from one end of the chain by hydrolysis of the peptide bond lead to the occurrence of the free carboxyl group and the free amino group that start from the opposite end 4 . This leads to greater absorption of natural dyes 5 and finally increases the hydrophilic property on the wool fabric 6 . Therefore, protease enzymes are used not only in the dyeing process, but also in improving the anti‐felt and anti‐pilling properties 7,8 .…”

Section: Introductionmentioning

confidence: 99%

“…4 This leads to greater absorption of natural dyes 5 and finally increases the hydrophilic property on the wool fabric. 6 Therefore, protease enzymes are used not only in the dyeing process, but also in improving the anti-felt and antipilling properties. 7,8 Enzymes are also used to improve dyeability and they are used for the pretreatment of wool.…”

Section: Introductionmentioning

confidence: 99%

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Eco‐friendly approach on wool pretreatment and effect on the wool structure and dyeability

Türkoğlu

Avcı

Erkan

et al. 2022

Coloration Technology

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This research investigated the effect of various proteolytic enzymatic pretreatment on morphological and chemical features and the dyeability properties of wool fibres. Scoured merino wool fibres are treated with protease, papain, trypsin, and pepsin in specified conditions. Each enzyme activity measurement was provided by appropriate methods such as Bradford, BAPNA (N-benzoyl-1-arginine-p-nitroanilide), and BSA (Bovine Serum Albumin). Enzymatic processes were carried out for 24 h in the incubator set at 40 C, 100 rpm, and specified pH with 1 mg/ml enzyme concentration. Whiteness index (Stensby) and yellowness index (ASTM D 1925) were examined after enzymatic pretreatment. Pepsin and trypsin-treated wool fibres showed the highest whiteness index as 61.3 and 61.1, respectively whilst untreated wool fibres had 52.2. Fourier-transform infrared (FTIR) analysis revealed the increase in the intensity of amide-related bands and hydroxyl bands after enzymatic treatment.Scanning electron microscopy (SEM) photomicrographs manifested the cuticle layer is partially removed in enzyme-treated fibres. Elemental identification was provided by SEM-energy-dispersive X-ray spectroscopy (EDX). It appears that the sulphur bonds decreased after the treatment and the pepsin-treated fibres have fewer bonds of all. To examine the damage to the structure, photomicrographs were taken using fluorescence and light microscopes. The alkali solubility test (ASTM D1283) was also conducted to compare different enzyme types. Wool fibres were dyed in 2.0% concentration with reactive dyestuff. Dyeability and colorimetric features of fibres were measured by a spectrophotometer. The washing fastness test showed that all the samples have good results and the colour change after washing was better in enzyme-treated samples (grade 5) compared to untreated wool fibres (grade 4-5).

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Insects as Valuable Sources of Protein and Peptides: Production, Functional Properties, and Challenges

Hasnan,

Feng,

Sun

et al. 2023

Foods

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As the global population approaches 10 billion by 2050, the critical need to ensure food security becomes increasingly pronounced. In response to the urgent problems posed by global population growth, our study adds to the growing body of knowledge in the field of alternative proteins, entomophagy, insect-based bioactive proteolysates, and peptides. It also provides novel insights with essential outcomes for guaranteeing a safe and sustainable food supply in the face of rising global population demands. These results offer insightful information to researchers and policymakers tackling the intricate relationship between population expansion and food supplies. Unfortunately, conventional agricultural practices are proving insufficient in meeting these demands. Pursuing alternative proteins and eco-friendly food production methods has gained urgency, embracing plant-based proteins, cultivated meat, fermentation, and precision agriculture. In this context, insect farming emerges as a promising strategy to upcycle agri-food waste into nutritious protein and fat, meeting diverse nutritional needs sustainably. A thorough analysis was conducted to evaluate the viability of insect farming, investigate insect nutrition, and review the techniques and functional properties of protein isolation. A review of peptide generation from insects was conducted, covering issues related to hydrolysate production, protein extraction, and peptide identification. The study addresses the nutritional value and global entomophagy habits to elucidate the potential of insects as sources of peptides and protein. This inquiry covers protein and hydrolysate production, highlighting techniques and bioactive peptides. Functional properties of insect proteins’ solubility, emulsification, foaming, gelation, water-holding, and oil absorption are investigated. Furthermore, sensory aspects of insect-fortified foods as well as challenges, including Halal and Kosher considerations, are explored across applications. Our review underscores insects’ promise as sustainable protein and peptide contributors, offering recommendations for further research to unlock their full potential.

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Enzymatic Hydrolysis of Proteins

Cited by 4 publications

References 0 publications

Freeze-Dried Tuna Pepsin Powder Stabilized by Some Cryoprotectants: In Vitro Simulated Gastric Digestion toward Different Proteins and Its Storage Stability

Freeze-Dried Tuna Pepsin Powder Stabilized by Some Cryoprotectants: In Vitro Simulated Gastric Digestion toward Different Proteins and Its Storage Stability

Eco‐friendly approach on wool pretreatment and effect on the wool structure and dyeability

Insects as Valuable Sources of Protein and Peptides: Production, Functional Properties, and Challenges

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