Naringinase

Naringinase is a complex of alpha-L-rhamnosidase and beta-D-glucosidase activities that hydrolyses naringin, the bitter flavanone glycoside of grapefruit and bitter orange, into the non-bitter aglycone naringenin and free sugars. It is the principal debittering enzyme of the citrus juice industry.

Light tan to off-white free-flowing powder. Activity is standardised in Naringinase Units (NU) defined as the amount of enzyme that hydrolyses one micromole of naringin per minute under defined assay conditions.

We supply food-grade Naringinase from manufacturers in China holding ISO 22000, Halal, Kosher and other certifications relevant to the product and production. Penicillium decumbens and Aspergillus niger are the dominant source organisms.

Common market grades include 500 NU/g standard juice-debittering grade, 2,000 NU/g concentrated for premium debittering applications, 10,000 NU/g high-activity grade, and dual-activity preparations balanced for both naringin and limonin removal.

Bulk and reduced-MOQ shipments. Batch-level COA covering activity, pH optimum, temperature optimum, moisture, heavy metals and microbiology.

Naringinase entered commercial food production in the 1960s and 1970s as the U.S. and Mediterranean grapefruit juice industries scaled and consumer preferences shifted toward less-bitter products. Early grapefruit varieties produced juice with naringin levels well above the 50 ppm bitterness threshold, making enzymatic debittering economically essential.

Industrial production is by submerged fermentation of Penicillium decumbens, Penicillium citrinum and Aspergillus niger strains. The enzyme is typically supplied as a blended preparation containing both rhamnosidase and glucosidase activities, since complete hydrolysis to non-bitter aglycone requires the sequential removal of both sugar units.

The enzyme is approved as a processing aid in the U.S. and EU citrus juice industries from approved source organisms, listed in the JECFA enzyme compendium, and supported by extensive safety documentation built up over decades of commercial use.

Mechanistically, naringinase first cleaves the alpha-L-rhamnoside bond to yield prunin (naringenin-7-O-glucoside), then cleaves the beta-D-glucoside bond to yield the non-bitter aglycone naringenin. Partial hydrolysis to prunin is itself a debittering step, since prunin is about one-third as bitter as the parent naringin.

Strategic positioning in industrial food processing is narrow but vital to the global citrus industry: naringinase is the enabling technology of commercial grapefruit juice production at scale, and emerging functional-ingredient applications (rhamnose, naringenin) add a second growth vector for the same enzyme.

• Grapefruit juice debittering; removes naringin-related bitterness from fresh and reconstituted juices
• Bitter orange juice processing; debittering of Seville orange and other bitter citrus varieties
• Citrus essential oil refinement; controls bitter flavanone carryover into peel oils
• Rhamnose production from naringin; commercial source of L-rhamnose for fine-chemical and flavour use
• Prunin production from naringin; intermediate for sweetener and flavour synthesis
• Wine processing where flavanone glycoside bitterness is undesirable
• Functional ingredient manufacture from citrus flavanones; controlled hydrolysis for aglycone-based products
• Tea processing where rhamnose-glucoside flavour compounds require modification