Effects of Ultrasound Assisted Extraction in Conjugation with Aid of Actinidin on the Molecular and Physicochemical Properties of Bovine Hide Gelatin

• Main Authors: Ahmad, SA (Author), Ahmad, T (Author), Awad, EA (Author), Imlan, JC (Author), Ismail, A (Author), Khalil, KA (Author), Leo, TK (Author), Sazili, AQ (Author)
• Format: Article
• Language: English
• Published: 2018
• Subjects: ACID PROTEASE; actinidin; BIGEYE SNAPPER; bovine hide; COLLAGEN; FISH GELATIN; FUNCTIONAL-PROPERTIES; GEL PROPERTIES; gel strength; gelatin; OPTIMIZATION; PEPSIN; PHYSICAL-PROPERTIES; physicochemical properties; SKIN GELATIN; ultrasound assisted extraction
• Online Access: View Fulltext in Publisher
• DOI: 10.3390/molecules23040730

Actinidin was used to pretreat the bovine hide and ultrasonic wave (53 kHz and 500 W) was used for the time durations of 2, 4 and 6 h at 60 degrees C to extract gelatin samples (UA2, UA4 and UA6, respectively). Control (UAC) gelatin was extracted using ultrasound for 6 h at 60 degrees C without enzyme pretreatment. There was significant (p < 0.05) increase in gelatin yield as the time duration of ultrasound treatment increased with UA6 giving the highest yield of 19.65%. Gel strength and viscosity of UAC and UA6 extracted gelatin samples were 627.53 and 502.16 g and 16.33 and 15.60 mPa.s, respectively. Longer duration of ultrasound treatment increased amino acids content of the extracted gelatin and UAC exhibited the highest content of amino acids. Progressive degradation of polypeptide chains was observed in the protein pattern of the extracted gelatin as the time duration of ultrasound extraction increased. Fourier transform infrared (FTIR) spectroscopy depicted loss of molecular order and degradation in UA6. Scanning electron microscopy (SEM) revealed protein aggregation and network formation in the gelatin samples with increasing time of ultrasound treatment. The study indicated that ultrasound assisted gelatin extraction using actinidin exhibited high yield with good quality gelatin.